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Human gmp synthetase - glutaminase domain

Analyse Human gmp synthetase - glutaminase domain in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2VPI
Type: protein
Length: 373 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Gmp synthase
EC: 6.3.5.2
UniProt: P49915
Pockets: 3 · best druggability 0.37

Structure

x-ray diffraction · 2 distinct chains · 24% helix, 31% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Gmp synthase (EC 6.3.5.2)	protein	187	24% helix, 31% strand	P49915
B	Gmp synthase (EC 6.3.5.2)	protein	186	24% helix, 31% strand	P49915

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	93	0.37	0.75	19	empty
2	57	0.34	0.77	13	empty
3	64	0.32	0.76	15	empty

Interfaces

1 interface between chains.

A–B · 609 Å² buried · 6 hydrogen bonds · protein-protein

Compared structures

2VPI · Human GMP synthetase - glutaminase domain · the same entry in another collection · chain A against A, TM-score 1.00
P49915 · AlphaFold monomer V2.0 prediction for gmp synthase [glutamine- hydrolyzing] (P49915) · a predicted model of the same protein · chain A against A, TM-score 0.97

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 P49915
Elsewhere: RCSB PDB 2VPI · PDBe 2VPI · UniProt P49915

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