MolNFT v1 · #15112 · protein

Structure of the 2-methylisocitrate lyase (prpb) from escherichia COLI

1MUM: “Structure of the 2-methylisocitrate lyase (prpb) from escherichia COLI”. X-ray diffraction, 1 ligand (MG), 2 pockets (best druggability 0.77). MolNFT v1 #15112 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 1MUM
Type: protein
Length: 578 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: 2-methylisocitrate lyase
EC: 4.1.3.30
UniProt: P77541
Ligands: MG
Pockets: 2 · best druggability 0.77

Structure

x-ray diffraction · 1 distinct chain · 51% helix, 13% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	2-methylisocitrate lyase (EC 4.1.3.30)	protein	289	51% helix, 13% strand	P77541

Ligands and binding sites

MG · Magnesium ion · metal · 2 copies · chains A, B

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

Pockets

2 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	743	0.77	0.81	66	MG
2	670	0.76	0.82	64	MG

Interfaces

1 interface between chains.

A–B · 3755 Å² buried · 53 hydrogen bonds · protein-protein

Compared structures

1MUM · Structure of the 2-Methylisocitrate Lyase (PrpB) from Escherichia coli · the same entry in another collection · chain A against A, TM-score 1.00
P77541 · AlphaFold monomer V2.0 prediction for 2-methylisocitrate lyase (P77541) · a predicted model of the same protein · chain A against A, TM-score 0.96

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 P77541
Elsewhere: RCSB PDB 1MUM · PDBe 1MUM · UniProt P77541

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