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Crystal structure of the catalase-peroxidase (katg) and S315T mutant from mycobacterium tuberculosis

Analyse Crystal structure of the catalase-peroxidase (katg) and S315T mutant from… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2CCA
Type: protein
Length: 1,430 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: PEROXIDASE/CATALASE T
EC: 1.11.1.6
UniProt: Q08129
Ligands: HEM
Pockets: 20 · best druggability 0.85

Structure

x-ray diffraction · 1 distinct chain · 46% helix, 7% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	PEROXIDASE/CATALASE T (EC 1.11.1.6)	protein	715	46% helix, 7% strand	Q08129

Ligands and binding sites

HEM · Protoporphyrin IX containing Fe · ligand · 2 copies · chains A, B

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

Pockets

20 pockets found on a 1 Å grid, 16 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	602	0.85	0.90	98	empty
2	557	0.83	0.88	65	HEM
3	547	0.82	0.87	65	HEM
4	232	0.78	0.92	35	empty
5	79	0.76	0.98	18	empty

Interfaces

1 interface between chains.

A–B · 4618 Å² buried · 40 hydrogen bonds · protein-protein

Compared structures

2CCA · Crystal structure of the catalase-peroxidase (KatG) and S315T mutant from Mycobacterium… · 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 Q08129
Elsewhere: RCSB PDB 2CCA · PDBe 2CCA · UniProt Q08129

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