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Crystal structure of the rhogap domain of ARHGAP11A

Analyse Crystal structure of the rhogap domain of ARHGAP11A in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3EAP
Type: protein
Length: 866 residues
Chains: 4
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Rho GTPase-activating protein 11A
UniProt: Q6P4F7
Ligands: UNX
Pockets: 14 · best druggability 0.83

Structure

x-ray diffraction · 4 distinct chains · 65% helix, 4% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Rho GTPase-activating protein 11A	protein	225	65% helix, 4% strand	Q6P4F7
B	Rho GTPase-activating protein 11A	protein	213	66% helix, 4% strand	Q6P4F7
C	Rho GTPase-activating protein 11A	protein	216	63% helix, 4% strand	Q6P4F7
D	Rho GTPase-activating protein 11A	protein	212	66% helix, 4% strand	Q6P4F7

Ligands and binding sites

UNX · Unknown atom or ion · ion · 6 copies · chains A, B, C

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

14 pockets found on a 1 Å grid, 8 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	1142	0.83	0.84	104	empty
2	651	0.74	0.80	62	UNX
3	558	0.73	0.81	44	empty
4	202	0.61	0.81	21	empty
5	126	0.58	0.85	23	empty

Interfaces

2 interfaces between chains.

A–D · 816 Å² buried · 7 hydrogen bonds · protein-protein
B–C · 674 Å² buried · 13 hydrogen bonds · protein-protein

Compared structures

3EAP · Crystal structure of the RhoGAP domain of ARHGAP11A · the same entry in another collection · chain D against D, TM-score 1.00
Q6P4F7 · AlphaFold monomer V2.0 prediction for rho GTPase-activating protein 11A (Q6P4F7) · a predicted model of the same protein · chain B against A, TM-score 0.99

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 Q6P4F7
Elsewhere: RCSB PDB 3EAP · PDBe 3EAP · UniProt Q6P4F7

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