Macromolecule Content

Total Structure Weight: 76.58 kDa
Atom Count: 4,349
Modelled Residue Count: 528
Deposited Residue Count: 666
Unique protein chains: 1

1MQB

Crystal Structure of Ephrin A2 (ephA2) Receptor Protein Kinase

PDB DOI: https://doi.org/10.2210/pdb1MQB/pdb

Classification: TRANSFERASE
Organism(s): Homo sapiens
Expression System: Spodoptera frugiperda
Mutation(s): No

Deposited: 2002-09-16 Released: 2003-09-16
Deposition Author(s): Nowakowski, J., Cronin, C.N., McRee, D.E., Knuth, M.W., Nelson, C., Pavletich, N., Rogers, J., Sang, B.C., Scheibe, D.N., Swanson, R.V., Thompson, D.A.

Experimental Data Snapshot

Method: X-RAY DIFFRACTION
Resolution: 2.30 Å
R-Value Free: 0.288
R-Value Work: 0.236
R-Value Observed: 0.236

wwPDB Validation 3D Report Full Report

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

Literature

Structures of the Cancer Related Aurora-A, FAK and EphA2 Protein Kinases from Nanovolume Crystallography

Nowakowski, J., Cronin, C.N., McRee, D.E., Knuth, M.W., Nelson, C., Pavletich, N., Rogers, J., Sang, B.C., Scheibe, D.N., Swanson, R.V., Thompson, D.A.

(2003) Structure 10: 1659-1667

PubMed: 12467573 Search on PubMed
DOI: https://doi.org/10.1016/s0969-2126(02)00907-3
Primary Citation of Related Structures:
1MP8, 1MQ4, 1MQB

PubMed Abstract:

Macromolecules

Find similar proteins by:

(by identity cutoff) | 3D Structure

Entity ID: 1
Molecule	Chains	Sequence Length	Organism	Details	Image
Ephrin type-A receptor 2	A, B	333	Homo sapiens	Mutation(s): 0 Gene Names: EPHA2, ECK EC: 2.7.1.112 (PDB Primary Data), 2.7.10.1 (UniProt)
UniProt & NIH Common Fund Data Resources
Find proteins for P29317 (Homo sapiens) Explore P29317 Go to UniProtKB: P29317
PHAROS: P29317
Entity Groups
Sequence Clusters	30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt Group	P29317
Protein Feature View Expand
Reference Sequence

Small Molecules

Ligands 1 Unique
ID	Chains	Name / Formula / InChI Key	2D Diagram	3D Interactions
ANP Query on ANP 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]	PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER C₁₀ H₁₇ N₆ O₁₂ P₃ PVKSNHVPLWYQGJ-KQYNXXCUSA-N		Ligand Interaction

Experimental Data & Validation

Experimental Data

Method: X-RAY DIFFRACTION
Resolution: 2.30 Å
R-Value Free: 0.288
R-Value Work: 0.236
R-Value Observed: 0.236
Space Group: P 3₂ 2 1

Unit Cell:

Length ( Å )	Angle ( ˚ )
a = 72.127	α = 90
b = 72.127	β = 90
c = 241.623	γ = 120

Software Package:

Software Name	Purpose
MOSFLM	data reduction
SCALA	data scaling
AMoRE	phasing
REFMAC	refinement
CCP4	data scaling

Structure Validation

View Full Validation Report

Entry History

Deposition Data

Released Date: 2003-09-16

Deposition Author(s):

Revision History (Full details and data files)

Version 1.0: 2003-09-16
Type: Initial release
Version 1.1: 2008-04-28
Changes: Version format compliance
Version 1.2: 2011-07-13
Changes: Version format compliance

RCSB PDB Core Operations are funded by the National Science Foundation (DBI-1832184), the US Department of Energy (DE-SC0019749), and the National Cancer Institute, National Institute of Allergy and Infectious Diseases, and National Institute of General Medical Sciences of the National Institutes of Health under grant R01GM133198.