MolNFT v1 · #19342 · protein

Escherichia COLI pyruvate formate lyase large domain

1QHM · Pyruvate formate-lyase: “Escherichia COLI pyruvate formate lyase large domain”. X-ray diffraction, 7 pockets (best druggability 0.85). MolNFT v1 #19342 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 1QHM
Type: protein
Length: 1,222 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Pyruvate formate-lyase
EC: 2.3.1.54
UniProt: P09373
Pockets: 7 · best druggability 0.85

Structure

x-ray diffraction · 1 distinct chain · 48% helix, 11% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Pyruvate formate-lyase (EC 2.3.1.54)	protein	611	48% helix, 11% strand	P09373

Pockets

7 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	1094	0.85	0.86	119	empty
2	334	0.60	0.77	55	empty
3	321	0.59	0.77	55	empty
4	211	0.56	0.79	25	empty
5	228	0.55	0.78	27	empty

Interfaces

1 interface between chains.

A–B · 2064 Å² buried · 35 hydrogen bonds · protein-protein

Compared structures

1QHM · Escherichia COLI pyruvate formate lyase large domain · the same entry in another collection · chain A against A, TM-score 1.00
P09373 · AlphaFold monomer V2.0 prediction for formate acetyltransferase 1 (P09373) · a predicted model of the same protein · chain A against A, TM-score 0.98

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 P09373
Elsewhere: RCSB PDB 1QHM · PDBe 1QHM · UniProt P09373

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