Research workbench

Crystal structure of human erythrocyte 2,3- bisphosphoglycerate mutase

Analyse Crystal structure of human erythrocyte 2,3- bisphosphoglycerate mutase in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1T8P
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
UniProt: P07738
Pockets: 5 · best druggability 0.68

Structure

x-ray diffraction · 1 distinct chain · 45% helix, 11% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Bisphosphoglycerate mutase (EC 5.4.2.4)	protein	249	45% helix, 11% strand	P07738

Pockets

5 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	423	0.68	0.80	51	empty
2	431	0.66	0.79	56	empty
3	381	0.63	0.78	49	empty
4	103	0.49	0.81	16	empty
5	72	0.36	0.77	16	empty

Interfaces

1 interface between chains.

A–B · 947 Å² buried · 9 hydrogen bonds · protein-protein

Compared structures

1T8P · Crystal structure of Human erythrocyte 2,3-bisphosphoglycerate mutase · 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 0.94

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 1T8P · PDBe 1T8P · UniProt P07738

GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.