2RCQ

Crystal structure of human apo Cellular Retinol Binding Protein II (CRBP-II)

PDB DOI: https://doi.org/10.2210/pdb2RCQ/pdb

Classification: RETINOL-BINDING PROTEIN
Organism(s): Homo sapiens
Expression System: Escherichia coli
Mutation(s): No

Deposited: 2007-09-20 Released: 2007-10-02
Deposition Author(s): Monaco, H.L., Capaldi, S., Perduca, M.

Experimental Data Snapshot

Method: X-RAY DIFFRACTION
Resolution: 1.20 Å
R-Value Free: 0.217
R-Value Work: 0.196
R-Value Observed: 0.197

Starting Model: experimental
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wwPDB Validation 3D Report Full Report

This is version 1.3 of the entry. See complete history.

Literature

Crystal structure of human cellular retinol-binding protein II to 1.2 A resolution.

Tarter, M., Capaldi, S., Carrizo, M.E., Ambrosi, E., Perduca, M., Monaco, H.L.

(2007) Proteins 70: 1626-1630

PubMed: 18076076 Search on PubMed
DOI: https://doi.org/10.1002/prot.21848
Primary Citation of Related Structures:
2RCQ, 2RCT

Organizational Affiliation

Department of Science and Technology, Biocrystallography Laboratory, University of Verona, Verona 37134, Italy.

Macromolecule Content

Total Structure Weight: 16.84 kDa
Atom Count: 1,348
Modelled Residue Count: 141
Deposited Residue Count: 141
Unique protein chains: 1

Macromolecules

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(by identity cutoff) | 3D Structure

Entity ID: 1
Molecule	Chains	Sequence Length	Organism	Details	Image
Retinol-binding protein II, cellular	A	141	Homo sapiens	Mutation(s): 0 Gene Names: RBP2, CRBP2
UniProt & NIH Common Fund Data Resources
Find proteins for P50120 (Homo sapiens) Explore P50120 Go to UniProtKB: P50120
PHAROS: P50120 GTEx: ENSG00000114113
Entity Groups
Sequence Clusters	30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt Group	P50120
Sequence Annotations Expand
Reference Sequence

Small Molecules

Ligands 2 Unique
ID	Chains	Name / Formula / InChI Key	2D Diagram	3D Interactions
TLA Query on TLA Download Ideal Coordinates CCD File SDF format, chain D [auth A] MOL2 format, chain D [auth A] mmCIF format, chain D [auth A]	D [auth A]	L(+)-TARTARIC ACID C₄ H₆ O₆ FEWJPZIEWOKRBE-JCYAYHJZSA-N		Interactions Focus chain D [auth A] Interactions & Density Focus chain D [auth A]
SO4 Query on SO4 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] mmCIF format, chain C [auth A] mmCIF format, chain B [auth A]	B [auth A], C [auth A]	SULFATE ION O₄ S QAOWNCQODCNURD-UHFFFAOYSA-L		Interactions Focus chain B [auth A] Focus chain C [auth A] Interactions & Density Focus chain B [auth A] Focus chain C [auth A]

Experimental Data & Validation

Experimental Data

Method: X-RAY DIFFRACTION
Resolution: 1.20 Å
R-Value Free: 0.217
R-Value Work: 0.196
R-Value Observed: 0.197
Space Group: P 2₁ 2₁ 2₁

Unit Cell:

Length ( Å )	Angle ( ˚ )
a = 35.518	α = 90
b = 49.834	β = 90
c = 74.398	γ = 90

Software Package:

Software Name	Purpose
REFMAC	refinement
PDB_EXTRACT	data extraction
MAR345dtb	data collection
MOSFLM	data reduction
SCALA	data scaling
MOLREP	phasing

Structure Validation

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Entry History

Deposition Data

Released Date: 2007-10-02

Deposition Author(s):

Monaco, H.L.

Capaldi, S.

Perduca, M.

Revision History (Full details and data files)

Version 1.0: 2007-10-02
Type: Initial release
Version 1.1: 2011-07-13
Changes: Version format compliance
Version 1.2: 2016-12-14
Changes: Structure summary
Version 1.3: 2023-08-30
Changes: Data collection, Database references, Derived calculations, Refinement description

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Help and Resources

2RCQ

Crystal structure of human apo Cellular Retinol Binding Protein II (CRBP-II)

Crystal structure of human cellular retinol-binding protein II to 1.2 A resolution.

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)