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Structure of KATE1 catalase from acinetobacter sp. VER3

Analyse Structure of KATE1 catalase from acinetobacter sp. VER3 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6PT7
Type: protein
Length: 500 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Catalase
UniProt: A0A031LXI5
Ligands: NAP, HEM, UNX, CL
Pockets: 6 · best druggability 0.76

Structure

x-ray diffraction · 1 distinct chain · 34% helix, 16% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Catalase	protein	500	34% helix, 16% strand	A0A031LXI5

Ligands and binding sites

NAP · Nadp nicotinamide-adenine-dinucleotide phosphate · ligand · chains A
HEM · Protoporphyrin IX containing Fe · ligand · chains A
UNX · Unknown atom or ion · ion · 3 copies · chains A
CL · Chloride ion · ion · chains A

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

Pockets

6 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	319	0.76	0.87	39	HEM
2	325	0.65	0.80	43	NAP
3	247	0.60	0.80	30	empty
4	282	0.51	0.74	47	empty
5	193	0.45	0.74	21	empty

Modifications

Observed in the structure: 1 modified (oxidation).

Compared structures

6PT7 · Structure of KatE1 catalase from Acinetobacter sp. Ver3 · 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 A0A031LXI5
Elsewhere: RCSB PDB 6PT7 · PDBe 6PT7 · UniProt A0A031LXI5

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