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Crystal structure of the YPT/RAB-gap domain of GYP1P

Analyse Crystal structure of the YPT/RAB-gap domain of GYP1P in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1FKM
Type: protein
Length: 322 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Protein (GYP1P)
UniProt: Q08484
Pockets: 3 · best druggability 0.45

Structure

x-ray diffraction · 1 distinct chain · 73% helix, 1% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Protein (GYP1P)	protein	322	73% helix, 1% strand	Q08484

Pockets

3 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	167	0.45	0.75	28	empty
2	94	0.37	0.75	26	empty
3	71	0.31	0.74	15	empty

Modifications

Observed in the structure: 8 modified (engineered).

Compared structures

1FKM · Crystal structure of the YPT/RAB-gap domain of GYP1P · the same entry in another collection · chain A against A, TM-score 1.00
Q08484 · AlphaFold monomer V2.0 prediction for GTPase-activating protein GYP1 (Q08484) · a predicted model of the same protein · chain A 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 Q08484
Elsewhere: RCSB PDB 1FKM · PDBe 1FKM · UniProt Q08484

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