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Crystal structure of clbq from the colibactin NRPS/PKS pathway

Analyse Crystal structure of clbq from the colibactin NRPS/PKS pathway in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5UGZ
Type: protein
Length: 478 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Putative thioesterase
UniProt: Q0P7K7
Pockets: 7 · best druggability 0.76

Structure

x-ray diffraction · 1 distinct chain · 44% helix, 15% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Putative thioesterase	protein	239	44% helix, 15% strand	Q0P7K7

Ligands and binding sites

BME · Beta-mercaptoethanol · additive · 2 copies · chains A, B

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

Pockets

7 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	886	0.76	0.79	73	BME
2	285	0.72	0.85	32	empty
3	93	0.71	0.94	23	empty
4	131	0.42	0.75	23	empty
5	61	0.37	0.79	17	empty

Interfaces

1 interface between chains.

A–B · 768 Å² buried · 8 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 1 covalent (additive adduct).

Compared structures

5UGZ · Crystal structure of ClbQ from the colibactin NRPS/PKS pathway · 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 Q0P7K7
Elsewhere: RCSB PDB 5UGZ · PDBe 5UGZ · UniProt Q0P7K7

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