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The structure of human bisphosphoglycerate mutase to 1.94A

Analyse The structure of human bisphosphoglycerate mutase to 1.94A in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3NFY
Type: protein
Length: 498 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Bisphosphoglycerate mutase
EC: 5.4.2.4, 5.4.2.1, 3.1.3.13
UniProt: P07738
Pockets: 6 · best druggability 0.67

Structure

x-ray diffraction · 1 distinct chain · 47% helix, 11% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Bisphosphoglycerate mutase (EC 5.4.2.4, 5.4.2.1, 3.1.3.13)	protein	249	47% helix, 11% strand	P07738

Pockets

6 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	262	0.67	0.84	38	empty
2	350	0.65	0.80	53	empty
3	398	0.63	0.77	46	empty
4	80	0.48	0.82	12	empty
5	78	0.35	0.76	17	empty

Interfaces

1 interface between chains.

A–B · 982 Å² buried · 11 hydrogen bonds · protein-protein

Compared structures

3NFY · The Structure of Human Bisphosphoglycerate Mutase to 1.94A · the same entry in another collection · chain A against A, TM-score 1.00
P07738 · AlphaFold monomer V2.0 prediction for bisphosphoglycerate mutase (P07738) · a predicted model of the same protein · chain A against A, TM-score 0.95

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 P07738
Elsewhere: RCSB PDB 3NFY · PDBe 3NFY · UniProt P07738

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