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Crystal structure of an engineered variant of single-chain penicillin G acylase from kluyvera cryocrescens (A1-ac RD3CHIS)

Analyse Crystal structure of an engineered variant of single-chain penicillin G acylase… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 7REP
Type: protein
Length: 764 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Penicillin G acylase
EC: 3.5.1.11
Ligands: PMS, CA
Pockets: 5 · best druggability 0.65

Structure

x-ray diffraction · 1 distinct chain · 35% helix, 21% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Penicillin G acylase (EC 3.5.1.11)	protein	764	35% helix, 21% strand	—

Ligands and binding sites

PMS · phenylmethanesulfonic acid · ligand · chains A
CA · Calcium ion · metal · 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, 3 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	632	0.65	0.75	65	empty
2	170	0.61	0.84	41	empty
3	51	0.50	0.87	19	empty
4	147	0.43	0.75	24	empty
5	113	0.39	0.75	19	empty

Modifications

Observed in the structure: 1 covalent (covalent ligand).

Compared structures

7REP · Crystal structure of an engineered variant of single-chain Penicillin G Acylase from… · 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
Elsewhere: RCSB PDB 7REP · PDBe 7REP

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