MolNFT v1 · #91004 · protein

Crystal structure of amidohydrolase from brucella melitensis

4F0L: “Crystal structure of amidohydrolase from brucella melitensis”. X-ray diffraction, 1 ligand (FE), 11 pockets (best druggability 0.76). MolNFT v1 #91004 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 4F0L
Type: protein
Length: 897 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Amidohydrolase
UniProt: Q2YIL4
Ligands: FE
Pockets: 11 · best druggability 0.76

Structure

x-ray diffraction · 2 distinct chains · 39% helix, 24% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Amidohydrolase	protein	448	39% helix, 24% strand	Q2YIL4
B	Amidohydrolase	protein	449	39% helix, 24% strand	Q2YIL4

Ligands and binding sites

FE · Fe (III) ion · metal · 2 copies · chains A, B
FMT · Formic acid · additive · 2 copies · chains A, B

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

Pockets

11 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	1014	0.76	0.79	61	empty
2	349	0.73	0.84	33	empty
3	337	0.72	0.84	31	empty
4	55	0.68	0.96	13	empty
5	202	0.57	0.80	38	FMT

Interfaces

1 interface between chains.

A–B · 2404 Å² buried · 59 hydrogen bonds · protein-protein

Compared structures

4F0L · Crystal structure of Amidohydrolase from Brucella melitensis · 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 Q2YIL4
Elsewhere: RCSB PDB 4F0L · PDBe 4F0L · UniProt Q2YIL4

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