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Phosphomannomutase from leishmania mexicana

Analyse Phosphomannomutase from leishmania mexicana in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2I54
Type: protein
Length: 726 residues
Chains: 3
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Phosphomannomutase
EC: 5.4.2.8
UniProt: Q95ZD7
Ligands: MG, CL
Pockets: 4 · best druggability 0.76

Structure

x-ray diffraction · 1 distinct chain · 42% helix, 21% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B, C	Phosphomannomutase (EC 5.4.2.8)	protein	242	42% helix, 21% strand	Q95ZD7

Ligands and binding sites

MG · Magnesium ion · metal · 3 copies · chains A, B, C
CL · Chloride ion · ion · 2 copies · chains A, B, C
CIT · Citric acid · additive · 3 copies · chains A, B, C

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

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	951	0.76	0.79	106	CIT, MG
2	617	0.67	0.76	53	empty
3	250	0.50	0.75	37	MG
4	108	0.42	0.77	21	empty

Interfaces

3 interfaces between chains.

B–C · 1074 Å² buried · 18 hydrogen bonds · protein-protein
A–B · 381 Å² buried · 3 hydrogen bonds · protein-protein
A–C · 11 Å² buried · 0 hydrogen bonds · protein-protein

Compared structures

2I54 · Phosphomannomutase from Leishmania mexicana · 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 Q95ZD7
Elsewhere: RCSB PDB 2I54 · PDBe 2I54 · UniProt Q95ZD7

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