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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: 2XFT
Type: protein
Length: 842 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: ORF12
UniProt: Q83Z62
Pockets: 12 · best druggability 0.74

Structure

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

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	ORF12	protein	418	46% helix, 22% strand	Q83Z62
B	ORF12	protein	424	45% helix, 21% 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

12 pockets found on a 1 Å grid, 6 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	527	0.74	0.82	52	GOL
2	495	0.73	0.82	51	GOL
3	284	0.66	0.82	50	empty
4	340	0.62	0.78	29	empty
5	272	0.61	0.79	30	empty

Interfaces

1 interface between chains.

A–B · 703 Å² buried · 3 hydrogen bonds · protein-protein

Compared structures

2XFT · 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

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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 2XFT · PDBe 2XFT · UniProt Q83Z62

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