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Di-haemic cytochrome C peroxidase from pseudomonas nautica 617, form in (pH 4.0)

Analyse Di-haemic cytochrome C peroxidase from pseudomonas nautica 617, form in (pH 4.0) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1NML
Type: protein
Length: 316 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Di-haem cytochrome C peroxidase
EC: 1.11.1.5
UniProt: P83787
Ligands: HEC
Pockets: 3 · best druggability 0.84

Structure

x-ray diffraction · 1 distinct chain · 40% helix, 8% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Di-haem cytochrome C peroxidase (EC 1.11.1.5)	protein	316	40% helix, 8% strand	P83787

Ligands and binding sites

HEC · Heme C · ligand · 2 copies · chains A
CIT · Citric acid · additive · 4 copies · chains A

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

Pockets

3 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	326	0.84	0.94	45	HEC, CIT
2	489	0.79	0.87	52	HEC, CIT
3	96	0.33	0.73	18	empty

Modifications

Observed in the structure: 4 cofactor (heme c attachment).

Compared structures

1NML · Di-haemic Cytochrome c Peroxidase from Pseudomonas nautica 617, form IN (pH 4.0) · 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 P83787
Elsewhere: RCSB PDB 1NML · PDBe 1NML · UniProt P83787

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