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Crystal structure of gar synthetase from aquifex aeolicus

Analyse Crystal structure of gar synthetase from aquifex aeolicus in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2YYA
Type: protein
Length: 846 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Phosphoribosylamine--glycine ligase
EC: 6.3.4.13
UniProt: O66949
Pockets: 7 · best druggability 0.76

Structure

x-ray diffraction · 1 distinct chain · 31% helix, 28% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Phosphoribosylamine--glycine ligase (EC 6.3.4.13)	protein	423	31% helix, 28% strand	O66949

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	836	0.76	0.80	75	empty
2	836	0.76	0.80	79	empty
3	337	0.58	0.76	36	empty
4	129	0.42	0.75	23	empty
5	114	0.41	0.76	23	empty

Interfaces

1 interface between chains.

A–B · 208 Å² buried · 2 hydrogen bonds · protein-protein

Compared structures

2YYA · Crystal structure of GAR synthetase from Aquifex aeolicus · the same entry in another collection · chain A against A, TM-score 1.00
O66949 · AlphaFold monomer V2.0 prediction for phosphoribosylamine--glycine ligase (O66949) · 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 O66949
Elsewhere: RCSB PDB 2YYA · PDBe 2YYA · UniProt O66949

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