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Crystal structure of an amidase (HYDANTOINASE/CARBAMOYLASE family) from burkholderia phymatum

Analyse Crystal structure of an amidase (HYDANTOINASE/CARBAMOYLASE family) from… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6C0D
Type: protein
Length: 404 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Amidase, HYDANTOINASE/CARBAMOYLASE family
EC: 3.5.1.87
UniProt: B2JR29
Ligands: ZN, SO4
Pockets: 1 · best druggability 0.49

Structure

x-ray diffraction · 1 distinct chain · 38% helix, 25% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Amidase, HYDANTOINASE/CARBAMOYLASE family (EC 3.5.1.87)	protein	404	38% helix, 25% strand	B2JR29

Ligands and binding sites

ZN · Zinc ion · metal · chains A
SO4 · Sulfate ion · ion · 2 copies · chains A
EDO · 1,2-ethanediol · additive · 7 copies · chains A
EPE · 4-(2-hydroxyethyl)-1-piperazine ethanesulfonic acid · additive · chains A

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

Pockets

1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	205	0.49	0.76	38	ZN

Compared structures

6C0D · Crystal structure of an Amidase (hydantoinase/carbamoylase family) from Burkholderia… · 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 B2JR29
Elsewhere: RCSB PDB 6C0D · PDBe 6C0D · UniProt B2JR29

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