MolNFT v1 · #71421 · protein

The structure of N-formimino-L-glutamate iminohydrolase from pseudomonas aeruginosa complexed with N-guanidino-L-glutamate

3MDU: “The structure of N-formimino-L-glutamate iminohydrolase from pseudomonas aeruginosa complexed with…”. X-ray diffraction, 2 ligands (NGQ, ZN), 5 pockets (best druggability 0.72). MolNFT v1 #71421 on GenesisL1: 3D structure, binding…

PDB: 3MDU
Type: protein
Length: 450 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: N-formimino-L-glutamate iminohydrolase
UniProt: Q9HU77
Ligands: NGQ, ZN
Pockets: 5 · best druggability 0.72

Structure

x-ray diffraction · 1 distinct chain · 42% helix, 22% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	N-formimino-L-glutamate iminohydrolase	protein	450	42% helix, 22% strand	Q9HU77

Ligands and binding sites

NGQ · N-carbamimidoyl-L-glutamic acid · ligand · chains A
ZN · Zinc ion · metal · chains A
GOL · Glycerol · additive · 2 copies · chains A

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

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	61	0.72	0.98	20	NGQ
2	60	0.36	0.78	17	empty
3	65	0.30	0.74	17	empty
4	51	0.28	0.75	14	empty
5	61	0.27	0.73	12	empty

Compared structures

3MDU · The structure of N-formimino-L-Glutamate Iminohydrolase from Pseudomonas aeruginosa… · 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
Every structure of UniProt Q9HU77
Elsewhere: RCSB PDB 3MDU · PDBe 3MDU · UniProt Q9HU77

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