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Crystal structure of the rasgap SH3 domain at 1.5 ångström resolution

Analyse Crystal structure of the rasgap SH3 domain at 1.5 ångström resolution in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2J05
Type: protein
Length: 123 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: RAS GTPase-activating protein 1
UniProt: P20936

Structure

x-ray diffraction · 2 distinct chains · 5% helix, 46% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	RAS GTPase-activating protein 1	protein	64	5% helix, 44% strand	P20936
B	RAS GTPase-activating protein 1	protein	59	5% helix, 47% strand	P20936

Interfaces

1 interface between chains.

A–B · 702 Å² buried · 12 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 5 modified (engineered).

Compared structures

2J05 · Crystal structure of the RasGAP SH3 domain at 1.5 Angstrom resolution · the same entry in another collection · chain A against A, TM-score 1.00
P20936 · AlphaFold monomer V2.0 prediction for RAS GTPase-activating protein 1 (P20936) · a predicted model of the same protein · chain B against A, TM-score 0.94

Analyse

Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
Every structure of UniProt P20936
Elsewhere: RCSB PDB 2J05 · PDBe 2J05 · UniProt P20936

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