2VUX

Human ribonucleotide reductase, subunit M2 B

PDB DOI: https://doi.org/10.2210/pdb2VUX/pdb

Classification: OXIDOREDUCTASE
Organism(s): Homo sapiens
Expression System: Escherichia coli BL21(DE3)
Mutation(s): No

Deposited: 2008-05-31 Released: 2008-07-15
Deposition Author(s): Welin, M., Moche, M., Andersson, J., Arrowsmith, C.H., Berglund, H., Busam, R.D., Collins, R., Dahlgren, L.G., Edwards, A.M., Flodin, S., Flores, A., Graslund, S., Hammarstrom, M., Herman, M.D., Johansson, A., Johansson, I., Kallas, A., Karlberg, T., Kotenyova, T., Lehtio, L., Nilsson, M.E., Nyman, T., Persson, C., Sagemark, J., Schueler, H., Svensson, L., Thorsell, A.G., Tresaugues, L., van Den Berg, S., Weigelt, J., Wikstrom, M., Nordlund, P., Structural Genomics Consortium (SGC)

Experimental Data Snapshot

Method: X-RAY DIFFRACTION
Resolution: 2.80 Å
R-Value Free: 0.258
R-Value Work: 0.209
R-Value Observed: 0.213

wwPDB Validation 3D Report Full Report

This is version 1.2 of the entry. See complete history.

Literature

Human Ribonucleotide Reductase, Subunit M2 B

Welin, M., Moche, M., Arrowsmith, C.H., Berglund, H., Busam, R.D., Collins, R., Dahlgren, L.G., Edwards, A.M., Flodin, S., Flores, A., Graslund, S., Hammarstrom, M., Herman, M.D., Johansson, A., Johansson, I., Kallas, A., Karlberg, T., Kotenyova, T., Lehtio, L., Nilsson, M.E., Nyman, T., Persson, C., Sagemark, J., Schueler, H., Svensson, L., Thorsell, A.G., Tresaugues, L., Van Den Berg, S., Weigelt, J., Wikstrom, M., Nordlund, P.

To be published.

Macromolecule Content

Total Structure Weight: 76.04 kDa
Atom Count: 4,362
Modelled Residue Count: 527
Deposited Residue Count: 652
Unique protein chains: 1

Macromolecules

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(by identity cutoff) | 3D Structure

Entity ID: 1
Molecule	Chains	Sequence Length	Organism	Details	Image
RIBONUCLEOSIDE-DIPHOSPHATE REDUCTASE SUBUNIT M2 B	A, B	326	Homo sapiens	Mutation(s): 0 EC: 1.17.4.1
UniProt & NIH Common Fund Data Resources
Find proteins for Q7LG56 (Homo sapiens) Explore Q7LG56 Go to UniProtKB: Q7LG56
PHAROS: Q7LG56 GTEx: ENSG00000048392
Entity Groups
Sequence Clusters	30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt Group	Q7LG56
Sequence Annotations Expand
Reference Sequence

Small Molecules

Ligands 1 Unique
ID	Chains	Name / Formula / InChI Key	2D Diagram	3D Interactions
FE Query on FE Download Ideal Coordinates CCD File SDF format, chain C [auth A] SDF format, chain D [auth B] MOL2 format, chain C [auth A] MOL2 format, chain D [auth B]	C [auth A], D [auth B]	FE (III) ION Fe VTLYFUHAOXGGBS-UHFFFAOYSA-N		Interactions Focus chain C [auth A] Focus chain D [auth B] Interactions & Density Focus chain C [auth A] Focus chain D [auth B]

Experimental Data & Validation

Experimental Data

Method: X-RAY DIFFRACTION
Resolution: 2.80 Å
R-Value Free: 0.258
R-Value Work: 0.209
R-Value Observed: 0.213
Space Group: P 2₁ 2₁ 2₁

Unit Cell:

Length ( Å )	Angle ( ˚ )
a = 68.96	α = 90
b = 99.47	β = 90
c = 132.58	γ = 90

Software Package:

Software Name	Purpose
REFMAC	refinement
XDS	data reduction
XSCALE	data scaling
MOLREP	phasing

Structure Validation

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Entry History

Deposition Data

Released Date: 2008-07-15

Deposition Author(s):

Structural Genomics Consortium (SGC)

Revision History (Full details and data files)

Version 1.0: 2008-07-15
Type: Initial release
Version 1.1: 2011-07-13
Changes: Advisory, Refinement description, Version format compliance
Version 1.2: 2023-12-13
Changes: Data collection, Database references, Derived calculations, Other, Refinement description

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Help and Resources

2VUX

Human ribonucleotide reductase, subunit M2 B

Human Ribonucleotide Reductase, Subunit M2 B

Entity ID: 1

UniProt & NIH Common Fund Data Resources

Entity Groups

Sequence Annotations

Expand

Experimental Data

Structure Validation

Deposition Data

Revision History (Full details and data files)