1B71

RUBRERYTHRIN

PDB DOI: https://doi.org/10.2210/pdb1B71/pdb

Classification: ELECTRON TRANSPORT
Organism(s): Nitratidesulfovibrio vulgaris str. Hildenborough
Mutation(s): No

Deposited: 1999-01-26 Released: 2000-01-26
Deposition Author(s): Sieker, L.C., Holmes, M., Le Trong, I., Turley, S., Santarsiero, B.D., Liu, M.-Y., Legall, J., Stenkamp, R.E.

Experimental Data Snapshot

Method: X-RAY DIFFRACTION
Resolution: 1.90 Å
R-Value Observed: 0.195

wwPDB Validation 3D Report Full Report

This is version 1.5 of the entry. See complete history.

Literature

Alternative metal-binding sites in rubrerythrin.

Sieker, L.C., Holmes, M., Le Trong, I., Turley, S., Santarsiero, B.D., Liu, M.Y., LeGall, J., Stenkamp, R.E.

(1999) Nat Struct Biol 6: 308-309

PubMed: 10201393 Search on PubMed
DOI: https://doi.org/10.1038/7538
Primary Citation of Related Structures:
1B71

Organizational Affiliation

Department of Biological Structure and Biomolecular Structure Center, University of Washington, Seattle 98195-7420, USA.

Macromolecule Content

Total Structure Weight: 21.75 kDa
Atom Count: 1,732
Modelled Residue Count: 191
Deposited Residue Count: 191
Unique protein chains: 1

Macromolecules

Find similar proteins by:

(by identity cutoff) | 3D Structure

Entity ID: 1
Molecule	Chains	Sequence Length	Organism	Details	Image
PROTEIN (RUBRERYTHRIN)	A	191	Nitratidesulfovibrio vulgaris str. Hildenborough	Mutation(s): 0
UniProt
Find proteins for P24931 (Desulfovibrio vulgaris (strain ATCC 29579 / DSM 644 / NCIMB 8303 / VKM B-1760 / Hildenborough)) Explore P24931 Go to UniProtKB: P24931
Entity Groups
Sequence Clusters	30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt Group	P24931
Sequence Annotations Expand
Reference Sequence

Small Molecules

Ligands 2 Unique
ID	Chains	Name / Formula / InChI Key	2D Diagram	3D Interactions
ZN Query on ZN Download Ideal Coordinates CCD File SDF format, chain D [auth A] MOL2 format, chain D [auth A]	D [auth A]	ZINC ION Zn PTFCDOFLOPIGGS-UHFFFAOYSA-N		Interactions Focus chain D [auth A]
FE Query on FE Download Ideal Coordinates CCD File SDF format, chain C [auth A] SDF format, chain B [auth A] MOL2 format, chain C [auth A] MOL2 format, chain B [auth A]	B [auth A], C [auth A]	FE (III) ION Fe VTLYFUHAOXGGBS-UHFFFAOYSA-N		Interactions Focus chain B [auth A] Focus chain C [auth A]

Experimental Data & Validation

Experimental Data

Method: X-RAY DIFFRACTION
Resolution: 1.90 Å
R-Value Observed: 0.195
Space Group: I 2 2 2

Unit Cell:

Length ( Å )	Angle ( ˚ )
a = 49.3	α = 90
b = 81.3	β = 90
c = 100.1	γ = 90

Software Package:

Software Name	Purpose
SHELXL-97	refinement

Structure Validation

View Full Validation Report

Entry History

Deposition Data

Released Date: 2000-01-26

Deposition Author(s):

Revision History (Full details and data files)

Version 1.0: 2000-01-26
Type: Initial release
Version 1.1: 2008-04-26
Changes: Version format compliance
Version 1.2: 2011-07-13
Changes: Derived calculations, Version format compliance
Version 1.3: 2014-10-29
Changes: Derived calculations
Version 1.4: 2017-10-04
Changes: Refinement description
Version 1.5: 2023-08-09
Changes: Data collection, Database references, Derived calculations, Refinement description

Prepare Data

Validate Data

Deposit Data

Help and Resources

1B71

RUBRERYTHRIN

Alternative metal-binding sites in rubrerythrin.

Entity ID: 1

UniProt

Entity Groups

Sequence Annotations

Expand

Experimental Data

Structure Validation

Deposition Data

Revision History (Full details and data files)