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Crystal structure of D-aminoacylase in complex with 100MM CUCL2

Analyse Crystal structure of D-aminoacylase in complex with 100MM CUCL2 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1RJP
Type: protein
Length: 474 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: D-aminoacylase
EC: 3.5.1.81
UniProt: Q9AGH8
Ligands: ZN, CU
Pockets: 2 · best druggability 0.71

Structure

x-ray diffraction · 1 distinct chain · 32% helix, 22% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	D-aminoacylase (EC 3.5.1.81)	protein	474	32% helix, 22% strand	Q9AGH8

Ligands and binding sites

ZN · Zinc ion · metal · chains A
CU · Copper (II) ion · metal · chains A
ACT · Acetate ion · additive · 2 copies · chains A

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

Pockets

2 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	57	0.71	0.98	22	ACT
2	96	0.35	0.74	17	empty

Compared structures

1RJP · Crystal structure of D-aminoacylase in complex with 100mM CuCl2 · 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 Q9AGH8
Elsewhere: RCSB PDB 1RJP · PDBe 1RJP · UniProt Q9AGH8

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