1AC8: VARIATION IN THE STRENGTH OF A CH TO O ... - RCSB PDB

Warning You are using a web browser that we do not support. Our website will not work properly. Please update to a newer version or download a new web browser, such as Chrome or Firefox. HelpContact usToggle navigationRCSB PDB

• Deposit

  Prepare Data

  • PDBx/mmCIF file
  • pdb_extract
  • SF-Tool
  • Ligand Expo
  • MAXIT

  Validate Data

  • Validation Server
  • Validation API
  • Information for Journals
  • Validation Task Forces

  Deposit Data

  • wwPDB OneDep System
  • PDB-IHM

  Help and Resources

  • Deposit FAQ
  • Validation FAQ
  • Tutorials
  • Annotation Policies
  • Processing Procedures
  • PDBx/mmCIF Dictionary
  • PDBx/mmCIF User Guide
  • Chemical Component Dictionary
  • Biologically Interesting Molecule Reference Dictionary (BIRD)
  • BioSync/Beamlines/Facilities
  • Related Tools
• Search
  • Advanced Search
  • Sequence Similarity Search
  • 3D Similarity Search
  • Chemical Similarity Search
  • Browse by Annotations
  • New Entries
  • Unreleased Entries
  • PDB Statistics
• Visualize
  • Mol* (MolStar)
  • Sequence Annotations Viewer
  • Genome View
• Analyze
  • Pairwise Structure Alignment
  • Symmetry Resources in the PDB
  • Structure Quality
  • Grouping Structures
  • PDB Citation MeSH Network Explorer
  • PDB Statistics
  • EPPIC Biological Assemblies
  • External Data and Resources
  • Integrated Resources
  • Additional Resources
• Download
  • Coordinates and Experimental Data
  • Sequences
  • Ligands
  • File Download Services
  • Web APIs
• Learn

  

  • Training Courses
  • Guide to PDB Data
  • Molecule of the Month
  • Educational Resources
  • Curricula
  • Browse
  • News
  • SciArt Galleries
  • Irving Geis
  • David Goodsell
• About
  • Contact Us
  • About RCSB PDB
  • Vision and Mission
  • Citation, Usage, Privacy Policies, Logo
  • News
  • PDB History
  • PDB50
  • User Community
  • Publications
  • RCSB PDB Advisory Committee
  • Team Members
  • Service Status
• Careers
• COVID-19

248,717Structures from the PDB archive 1,068,577Computed Structure Models (CSM)

• 
• 
• 
• 
• 
• 

Navigation Tabs

• Structure Summary
• Structure
• Annotations
• Experiment
• Sequence
• Genome
• Versions

Display Files

• FASTA Sequence
• mmCIF Format
• mmCIF Format (Header)
• Legacy PDB Format
• Legacy PDB Format (Header)

Download Files

• FASTA Sequence
• PDBx/mmCIF Format
• PDBx/mmCIF Format (gz)
• BinaryCIF Format (gz)
• Legacy PDB Format
• Legacy PDB Format (gz)
• PDBML/XML Format (gz)
• Structure Factors (CIF)
• Structure Factors (CIF - gz)
• Validation Full (PDF - gz)
• Validation (XML - gz)
• Validation (CIF - gz)
• Validation 2fo-fc coefficients (CIF - gz)
• Validation fo-fc coefficients (CIF - gz)
• Biological Assembly 1 (CIF - gz)
• Biological Assembly 1 (PDB - gz)

Data API 1AC8 | pdb_00001ac8

VARIATION IN THE STRENGTH OF A CH TO O HYDROGEN BOND IN AN ARTIFICIAL PROTEIN CAVITY (3,4,5-TRIMETHYLTHIAZOLE)

• PDB DOI: https://doi.org/10.2210/pdb1AC8/pdb

• Classification: OXIDOREDUCTASE
• Organism(s): Saccharomyces cerevisiae
• Expression System: Escherichia coli BL21(DE3)
• Mutation(s): Yes 
• Deposited: 1997-02-14 Released: 1997-09-04 
• Deposition Author(s): Musah, R.A., Jensen, G.M., Bunte, S.W., Rosenfeld, R., Mcree, D.E., Goodin, D.B.

Experimental Data Snapshot

• Method: X-RAY DIFFRACTION
• Resolution: 2.10 Å
• R-Value Work:  0.210 (DCC) 

Starting Model: experimentalView more details

wwPDB Validation   3D Report Full Report

This is version 1.5 of the entry. See complete history. LiteratureDownload Primary Citation 

•  Download Mendeley

Variation in strength of an unconventional C-H to O hydrogen bond in an engineered protein cavity

Fitzgerald, M.M., Musah, R.A., McRee, D.E., Goodin, D.B.

(1997) J Am Chem Soc 119: 626-631

Asymmetric Unit

 Explore in 3D: Structure | Sequence Annotations | Electron Density | Validation Report | Ligand Interaction (HEM)

Biological Assembly 1  

 Explore in 3D: Structure | Sequence Annotations | Electron Density | Validation Report | Ligand Interaction (HEM)

Global Symmetry: Asymmetric - C1 Global Stoichiometry: Monomer - A1 LessFind Similar Assemblies

Biological assembly 1 assigned by authors.

PreviousNext

Macromolecule Content 

• Total Structure Weight: 34.2 kDa 
• Atom Count: 2,489 
• Modeled Residue Count: 291 
• Deposited Residue Count: 294 
• Unique protein chains: 1

MacromoleculesFind similar proteins by: Sequence

• 100%
• 95%
• 90%
• 80%
• 70%
• 60%
• 50%
• 40%
• 30%

(by identity cutoff) | 3D Structure

Entity ID: 1
Molecule	Chains	Sequence Length	Organism	Details	Image
CYTOCHROME C PEROXIDASE	A	294	Saccharomyces cerevisiae	Mutation(s): 1 Gene Names: CCPEC: 1.11.1.5
UniProt
Find proteins for P00431 (Saccharomyces cerevisiae (strain ATCC 204508 / S288c))Explore P00431 Go to UniProtKB:  P00431
Entity Groups
Sequence Clusters	30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt Group	P00431
Sequence Annotations Expand
Reference Sequence

Small Molecules

Ligands 2 Unique
ID	Chains	Name / Formula / InChI Key	2D Diagram	3D Interactions
HEMQuery on HEMDownload Ideal Coordinates CCD File Download Instance Coordinates SDF format, chain B [auth A] MOL2 format, chain B [auth A] mmCIF format, chain B [auth A]	B [auth A]	PROTOPORPHYRIN IX CONTAINING FEC34 H32 Fe N4 O4KABFMIBPWCXCRK-RGGAHWMASA-L		Interactions Focus chain B [auth A] Interactions & Density Focus chain B [auth A]
TMZQuery on TMZDownload Ideal Coordinates CCD File Download Instance Coordinates SDF format, chain C [auth A] MOL2 format, chain C [auth A] mmCIF format, chain C [auth A]	C [auth A]	3,4,5-TRIMETHYL-1,3-THIAZOLEC6 H10 N SLTPCOIDSGQEHKC-UHFFFAOYSA-N		Interactions Focus chain C [auth A] Interactions & Density Focus chain C [auth A]

Experimental Data & Validation

Experimental Data

• Method: X-RAY DIFFRACTION
• Resolution: 2.10 Å
• R-Value Work:  0.210 (DCC) 

Space Group: P 21 21 21Unit Cell:

Length ( Å )	Angle ( ˚ )
a = 108	α = 90
b = 77.3	β = 90
c = 51.8	γ = 90

Software Package:

Software Name	Purpose
XTALVIEW	refinement
XENGEN	data reduction
XENGEN	data scaling

Structure Validation

View Full Validation Report

View more in-depth experimental dataEntry History 

Deposition Data

• Released Date: 1997-09-04 
Deposition Author(s): Musah, R.A., Jensen, G.M., Bunte, S.W., Rosenfeld, R., Mcree, D.E., Goodin, D.B.

Revision History (Full details and data files)

• Version 1.0: 1997-09-04Type: Initial release
• Version 1.1: 2008-03-04Changes: Version format compliance
• Version 1.2: 2011-07-13Changes: Version format compliance
• Version 1.3: 2021-11-03Changes: Database references, Derived calculations
• Version 1.4: 2023-08-02Changes: Refinement description
• Version 1.5: 2024-05-22Changes: Data collection

• About
• About Us
• Citing Us
• Publications
• Team
• Careers
• Usage & Privacy

• Support
• Contact Us
• Help
• Website FAQ
• Glossary
• Service Status

• RCSB PDB is hosted by
• 

• RCSB PDB is a member of
• 
• RCSB Partners
• Nucleic Acid Knowledgebase

• wwPDB Partners
• RCSB PDB
• PDBe
• PDBj
• BMRB
• EMDB

RCSB PDB Core Operations are funded by the U.S. National Science Foundation (DBI-2321666), the US Department of Energy (DE-SC0019749), and the National Cancer Institute, National Institute of Allergy and Infectious Diseases, and National Institute of General Medical Sciences of the National Institutes of Health under grant R01GM157729. RCSB PDB uses resources of the National Energy Research Scientific Computing Center (NERSC), a Department of Energy User Facility.