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Peroxide-bound dico-sulerythrin

Analyse Peroxide-bound dico-sulerythrin in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 7O9D
Type: protein
Length: 284 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Sulerythrin
UniProt: F9VPE5
Ligands: PEO, CO, CL
Pockets: 2 · best druggability 0.38

Structure

x-ray diffraction · 2 distinct chains · 81% helix, 0% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Sulerythrin	protein	141	82% helix, 0% strand	F9VPE5
B	Sulerythrin	protein	143	80% helix, 0% strand	F9VPE5

Ligands and binding sites

PEO · Hydrogen peroxide · ligand · 2 copies · chains A, B
CO · Cobalt (II) ion · metal · 5 copies · chains A, B
CL · Chloride ion · ion · 2 copies · chains A, B

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

Pockets

2 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	55	0.38	0.80	17	empty
2	76	0.36	0.77	18	empty

Interfaces

1 interface between chains.

A–B · 3500 Å² buried · 53 hydrogen bonds · protein-protein

Compared structures

7O9D · peroxide-bound diCo-sulerythrin · 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 F9VPE5
Elsewhere: RCSB PDB 7O9D · PDBe 7O9D · UniProt F9VPE5

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