256B

IMPROVEMENT OF THE 2.5 ANGSTROMS RESOLUTION MODEL OF CYTOCHROME B562 BY REDETERMINING THE PRIMARY STRUCTURE AND USING MOLECULAR GRAPHICS

PDB DOI: https://doi.org/10.2210/pdb256B/pdb
Entry: 256B supersedes: 156B

Classification: ELECTRON TRANSPORT
Organism(s): Escherichia coli
Mutation(s): No

Deposited: 1990-01-16 Released: 1991-01-15
Deposition Author(s): Hamada, K., Bethge, P.H., Mathews, F.S.

Experimental Data Snapshot

Method: X-RAY DIFFRACTION
Resolution: 1.40 Å
R-Value Observed: 0.164

wwPDB Validation 3D Report Full Report

Ligand Structure Quality Assessment

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

Literature

Improvement of the 2.5 A resolution model of cytochrome b562 by redetermining the primary structure and using molecular graphics.

Lederer, F., Glatigny, A., Bethge, P.H., Bellamy, H.D., Matthew, F.S.

(1981) J Mol Biol 148: 427-448

PubMed: 7031264 Search on PubMed
DOI: https://doi.org/10.1016/0022-2836(81)90185-6
Primary Citation of Related Structures:
256B

Macromolecule Content

Total Structure Weight: 25.22 kDa
Atom Count: 1,923
Modelled Residue Count: 212
Deposited Residue Count: 212
Unique protein chains: 1

Macromolecules

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(by identity cutoff) | 3D Structure

Entity ID: 1
Molecule	Chains	Sequence Length	Organism	Details	Image
CYTOCHROME B562	A, B	106	Escherichia coli	Mutation(s): 0
UniProt
Find proteins for P0ABE7 (Escherichia coli) Explore P0ABE7 Go to UniProtKB: P0ABE7
Entity Groups
Sequence Clusters	30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt Group	P0ABE7
Sequence Annotations Expand
Reference Sequence

Small Molecules

Ligands 2 Unique
ID	Chains	Name / Formula / InChI Key	2D Diagram	3D Interactions
HEM Query on HEM Download Ideal Coordinates CCD File SDF format, chain E [auth A] SDF format, chain H [auth B] MOL2 format, chain E [auth A] MOL2 format, chain H [auth B] mmCIF format, chain E [auth A] mmCIF format, chain H [auth B]	E [auth A], H [auth B]	PROTOPORPHYRIN IX CONTAINING FE C₃₄ H₃₂ Fe N₄ O₄ KABFMIBPWCXCRK-RGGAHWMASA-L		Interactions Focus chain E [auth A] Focus chain H [auth B] Interactions & Density Focus chain E [auth A] Focus chain H [auth B]
SO4 Query on SO4 Download Ideal Coordinates CCD File SDF format, chain G [auth B] SDF format, chain C [auth A] SDF format, chain D [auth A] SDF format, chain F [auth B] MOL2 format, chain G [auth B] MOL2 format, chain C [auth A] MOL2 format, chain D [auth A] MOL2 format, chain F [auth B] mmCIF format, chain G [auth B] mmCIF format, chain C [auth A] mmCIF format, chain D [auth A] mmCIF format, chain F [auth B]	C [auth A], D [auth A], F [auth B], G [auth B]	SULFATE ION O₄ S QAOWNCQODCNURD-UHFFFAOYSA-L		Interactions Focus chain C [auth A] Focus chain D [auth A] Focus chain F [auth B] Focus chain G [auth B] Interactions & Density Focus chain C [auth A] Focus chain D [auth A] Focus chain F [auth B] Focus chain G [auth B]

Experimental Data & Validation

Experimental Data

Method: X-RAY DIFFRACTION
Resolution: 1.40 Å
R-Value Observed: 0.164
Space Group: P 1

Unit Cell:

Length ( Å )	Angle ( ˚ )
a = 33.71	α = 102.76
b = 50.48	β = 86.55
c = 32.73	γ = 106.7

Software Package:

Software Name	Purpose
PROFFT	refinement

Structure Validation

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Ligand Structure Quality Assessment

Entry History

Deposition Data

Released Date: 1991-01-15

Deposition Author(s):

Hamada, K.

Bethge, P.H.

Mathews, F.S.

This entry supersedes: 156B

Revision History (Full details and data files)

Version 1.0: 1991-01-15
Type: Initial release
Version 1.1: 2008-03-03
Changes: Version format compliance
Version 1.2: 2011-07-13
Changes: Version format compliance
Version 1.3: 2014-08-27
Changes: Derived calculations
Version 1.4: 2017-11-29
Changes: Derived calculations, Other
Version 1.5: 2024-02-14
Changes: Data collection, Database references, Derived calculations

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256B

IMPROVEMENT OF THE 2.5 ANGSTROMS RESOLUTION MODEL OF CYTOCHROME B562 BY REDETERMINING THE PRIMARY STRUCTURE AND USING MOLECULAR GRAPHICS

Improvement of the 2.5 A resolution model of cytochrome b562 by redetermining the primary structure and using molecular graphics.

Entity ID: 1

UniProt

Entity Groups

Sequence Annotations

Expand

Experimental Data

Structure Validation

Ligand Structure Quality Assessment

Deposition Data

Revision History (Full details and data files)