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Crystal structure of phosphoglycerate mutase from staphylococcus aureus in 2-phosphoglyceric acid bound form

Analyse Crystal structure of phosphoglycerate mutase from staphylococcus aureus in… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4NWX
Type: protein
Length: 503 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: 2,3-bisphosphoglycerate-independent phosphoglycerate mutase
EC: 5.4.2.12
UniProt: Q2G029
Ligands: 2PG, MN
Pockets: 1 · best druggability 0.59

Structure

x-ray diffraction · 1 distinct chain · 39% helix, 16% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	2,3-bisphosphoglycerate-independent phosphoglycerate mutase (EC 5.4.2.12)	protein	503	39% helix, 16% strand	Q2G029

Ligands and binding sites

2PG · 2-phosphoglyceric acid · ligand · chains A
MN · Manganese (II) ion · metal · 2 copies · chains A
DTT · 2,3-dihydroxy-1,4-dithiobutane · additive · chains A

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

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	411	0.59	0.75	38	empty

Compared structures

4NWX · Crystal structure of phosphoglycerate mutase from Staphylococcus aureus in… · 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 Q2G029
Elsewhere: RCSB PDB 4NWX · PDBe 4NWX · UniProt Q2G029

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