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Structural and mechanistic studies on a cephalosporin esterase from the clavulanic acid biosynthesis pathway

Analyse Structural and mechanistic studies on a cephalosporin esterase from the… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2XGN
Type: protein
Length: 844 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: ORF12
UniProt: Q83Z62
Pockets: 13 · best druggability 0.73

Structure

x-ray diffraction · 2 distinct chains · 45% helix, 22% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	ORF12	protein	420	45% helix, 22% strand	Q83Z62
B	ORF12	protein	424	44% helix, 22% strand	Q83Z62

Ligands and binding sites

GOL · Glycerol · additive · 2 copies · chains A, B

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

Pockets

13 pockets found on a 1 Å grid, 7 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	530	0.73	0.82	56	GOL
2	503	0.73	0.82	53	GOL
3	60	0.71	0.98	25	empty
4	336	0.63	0.78	28	empty
5	334	0.62	0.78	34	empty

Interfaces

1 interface between chains.

A–B · 743 Å² buried · 5 hydrogen bonds · protein-protein

Compared structures

2XGN · Structural and mechanistic studies on a cephalosporin esterase from the clavulanic acid… · 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 Q83Z62
Elsewhere: RCSB PDB 2XGN · PDBe 2XGN · UniProt Q83Z62

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