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Crystal structure of oligomeric E.COLI guanylate kinase in complex with gmp

Analyse Crystal structure of oligomeric E.COLI guanylate kinase in complex with gmp in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2ANB
Type: protein
Length: 206 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Guanylate kinase
EC: 2.7.4.8
UniProt: P60546
Ligands: 5GP, SO4
Pockets: 2 · best druggability 0.72

Structure

x-ray diffraction · 1 distinct chain · 46% helix, 21% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Guanylate kinase (EC 2.7.4.8)	protein	206	46% helix, 21% strand	P60546

Ligands and binding sites

5GP · Guanosine-5'-monophosphate · ligand · chains A
SO4 · Sulfate ion · ion · chains A

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

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	375	0.72	0.84	46	SO4, 5GP
2	82	0.36	0.76	19	empty

Compared structures

2ANB · Crystal Structure Of Oligomeric E.coli Guanylate Kinase In Complex With GMP · the same entry in another collection · chain A against A, TM-score 1.00
P60546 · AlphaFold monomer V2.0 prediction for guanylate kinase (P60546) · a predicted model of the same protein · chain A against A, TM-score 0.83

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 P60546
Elsewhere: RCSB PDB 2ANB · PDBe 2ANB · UniProt P60546

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