MolNFT v1 · #24688 · protein

Crystal structure of phosphoglycerate mutase from thermus thermophilus HB8

1V37: “Crystal structure of phosphoglycerate mutase from thermus thermophilus HB8”. X-ray diffraction, 5 pockets (best druggability 0.68). MolNFT v1 #24688 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 1V37
Type: protein
Length: 341 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Phosphoglycerate mutase
EC: 5.4.2.1
UniProt: Q53WB3
Pockets: 5 · best druggability 0.68

Structure

x-ray diffraction · 2 distinct chains · 38% helix, 17% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Phosphoglycerate mutase (EC 5.4.2.1)	protein	171	38% helix, 17% strand	Q53WB3
B	Phosphoglycerate mutase (EC 5.4.2.1)	protein	170	37% helix, 17% strand	Q53WB3

Ligands and binding sites

GOL · Glycerol · additive · 2 copies · chains A, B

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

Pockets

5 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	271	0.68	0.83	30	empty
2	297	0.67	0.82	30	empty
3	71	0.56	0.88	24	empty
4	81	0.51	0.84	17	GOL
5	66	0.29	0.74	17	empty

Interfaces

1 interface between chains.

A–B · 704 Å² buried · 9 hydrogen bonds · protein-protein

Compared structures

1V37 · Crystal structure of phosphoglycerate mutase from Thermus thermophilus HB8 · the same entry in another collection · chain A against A, TM-score 1.00

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 Q53WB3
Elsewhere: RCSB PDB 1V37 · PDBe 1V37 · UniProt Q53WB3

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