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Structure of phosphoglycerate mutase from plasmodium falciparum at 2.6 resolution

Analyse Structure of phosphoglycerate mutase from plasmodium falciparum at 2.6… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1XQ9
Type: protein
Length: 481 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Phosphoglycerate mutase
Ligands: SCN
Pockets: 7 · best druggability 0.65

Structure

x-ray diffraction · 2 distinct chains · 43% helix, 14% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Phosphoglycerate mutase	protein	241	43% helix, 14% strand	—
B	Phosphoglycerate mutase	protein	240	43% helix, 14% strand	—

Ligands and binding sites

SCN · Thiocyanate ion · ion · 3 copies · chains A, B

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

Pockets

7 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	377	0.65	0.79	42	SCN
2	407	0.64	0.79	36	SCN
3	150	0.51	0.79	23	empty
4	217	0.51	0.76	32	empty
5	95	0.40	0.77	22	empty

Interfaces

1 interface between chains.

A–B · 837 Å² buried · 12 hydrogen bonds · protein-protein

Compared structures

1XQ9 · Structure of Phosphoglycerate Mutase from Plasmodium falciparum at 2.6 Resolution · 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
Elsewhere: RCSB PDB 1XQ9 · PDBe 1XQ9

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