1EPA

STRUCTURE OF THE EPIDIDYMAL RETINOIC ACID-BINDING PROTEIN AT 2.1 ANGSTROMS RESOLUTION

PDB DOI: https://doi.org/10.2210/pdb1EPA/pdb

Classification: RETINOIC ACID-BINDING PROTEIN
Organism(s): Rattus norvegicus
Mutation(s): No

Deposited: 1993-06-15 Released: 1994-07-31
Deposition Author(s): Newcomer, M.E.

Experimental Data Snapshot

Method: X-RAY DIFFRACTION
Resolution: 2.10 Å
R-Value Work: 0.196
R-Value Observed: 0.196

wwPDB Validation 3D Report Full Report

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

Literature

Structure of the epididymal retinoic acid binding protein at 2.1 A resolution.

(1993) Structure 1: 7-18

PubMed: 8069623 Search on PubMed
DOI: https://doi.org/10.1016/0969-2126(93)90004-z
Primary Citation of Related Structures:
1EPA, 1EPB

PubMed Abstract:
Androgen-dependent proteins in the lumen of the epididymis are required for sperm maturation. One of these is a retinoic acid binding protein, E-RABP, which binds both all-trans and 9-cis retinoic acid. The other retinoid-binding proteins whose structures are known do not bind 9-cis retinoids.

Organizational Affiliation

Department of Biochemistry, Vanderbilt University School of Medicine, Nashville, Tennessee 37232-0146.

Macromolecule Content

Total Structure Weight: 36.5 kDa
Atom Count: 2,549
Modelled Residue Count: 324
Deposited Residue Count: 328
Unique protein chains: 1

Macromolecules

Find similar proteins by:

(by identity cutoff) | 3D Structure

Entity ID: 1
Molecule	Chains	Sequence Length	Organism	Details	Image
EPIDIDYMAL RETINOIC ACID-BINDING PROTEIN	A, B	164	Rattus norvegicus	Mutation(s): 0
UniProt
Find proteins for P06911 (Rattus norvegicus) Explore P06911 Go to UniProtKB: P06911
Entity Groups
Sequence Clusters	30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt Group	P06911
Sequence Annotations Expand
Reference Sequence

Experimental Data & Validation

Experimental Data

Method: X-RAY DIFFRACTION
Resolution: 2.10 Å
R-Value Work: 0.196
R-Value Observed: 0.196
Space Group: P 1 2₁ 1

Unit Cell:

Length ( Å )	Angle ( ˚ )
a = 39.33	α = 90
b = 58.67	β = 109.34
c = 66.27	γ = 90

Software Package:

Software Name	Purpose
X-PLOR	model building
X-PLOR	refinement
X-PLOR	phasing

Structure Validation

View Full Validation Report

Entry History

Deposition Data

Released Date: 1994-07-31

Deposition Author(s):

Revision History (Full details and data files)

Version 1.0: 1994-07-31
Type: Initial release
Version 1.1: 2008-03-24
Changes: Version format compliance
Version 1.2: 2011-07-13
Changes: Version format compliance
Version 1.3: 2017-11-29
Changes: Derived calculations, Other

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