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Dimn-sulerythrin

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

PDB: 7O91
Type: protein
Length: 429 residues
Chains: 3
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Sulerythrin
UniProt: F9VPE5
Ligands: MN, CL
Pockets: 3 · best druggability 0.47

Structure

x-ray diffraction · 3 distinct chains · 80% helix, 0% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Sulerythrin	protein	146	79% helix, 0% strand	F9VPE5
B	Sulerythrin	protein	139	81% helix, 0% strand	F9VPE5
C	Sulerythrin	protein	144	81% helix, 0% strand	F9VPE5

Ligands and binding sites

MN · Manganese (II) ion · metal · 6 copies · chains A, B, C
CL · Chloride ion · ion · 3 copies · chains A, B, C
PEG · Di(hydroxyethyl)ether · additive · 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, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	211	0.47	0.74	34	empty
2	55	0.41	0.82	21	empty
3	80	0.29	0.72	17	empty

Interfaces

2 interfaces between chains.

B–C · 3526 Å² buried · 52 hydrogen bonds · protein-protein
A–B · 266 Å² buried · 2 hydrogen bonds · protein-protein

Compared structures

7O91 · diMn-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 7O91 · PDBe 7O91 · UniProt F9VPE5

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