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Crystal structure of apo phosphoenolpyruvate mutase

Analyse Crystal structure of apo phosphoenolpyruvate mutase in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1S2T
Type: protein
Length: 582 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Phosphoenolpyruvate phosphomutase
EC: 5.4.2.9
UniProt: P56839
Pockets: 5 · best druggability 0.59

Structure

x-ray diffraction · 2 distinct chains · 47% helix, 12% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Phosphoenolpyruvate phosphomutase (EC 5.4.2.9)	protein	291	46% helix, 12% strand	P56839
B	Phosphoenolpyruvate phosphomutase (EC 5.4.2.9)	protein	291	49% helix, 12% strand	P56839

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	364	0.59	0.76	40	empty
2	332	0.58	0.77	39	empty
3	453	0.56	0.73	47	empty
4	131	0.55	0.82	21	empty
5	199	0.43	0.73	16	empty

Interfaces

1 interface between chains.

A–B · 1135 Å² buried · 13 hydrogen bonds · protein-protein

Compared structures

1S2T · Crystal Structure Of Apo Phosphoenolpyruvate Mutase · the same entry in another collection · chain A against A, TM-score 1.00
P56839 · AlphaFold monomer V2.0 prediction for phosphoenolpyruvate phosphomutase (P56839) · a predicted model of the same protein · chain B against A, TM-score 0.96

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 P56839
Elsewhere: RCSB PDB 1S2T · PDBe 1S2T · UniProt P56839

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