MolNFT v1 · #185320 · protein

Structure of dife-sulerythrin at 2.70 mgy total absorbed dose

7PPV: “Structure of dife-sulerythrin at 2.70 mgy total absorbed dose”. X-ray diffraction, 3 ligands (FE, CL, OH), 2 pockets (best druggability 0.44). MolNFT v1 #185320 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 7PPV
Type: protein
Length: 283 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Sulerythrin
UniProt: F9VPE5
Ligands: FE, CL, OH
Pockets: 2 · best druggability 0.44

Structure

x-ray diffraction · 2 distinct chains · 81% helix, 1% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Sulerythrin	protein	142	80% helix, 1% strand	F9VPE5
B	Sulerythrin	protein	141	81% helix, 0% strand	F9VPE5

Ligands and binding sites

FE · Fe (III) ion · metal · 4 copies · chains A, B
CL · Chloride ion · ion · 2 copies · chains A, B
OH · Hydroxide 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	75	0.44	0.81	18	empty
2	68	0.38	0.79	16	empty

Interfaces

1 interface between chains.

A–B · 3455 Å² buried · 47 hydrogen bonds · protein-protein

Compared structures

7PPV · Structure of diFe-Sulerythrin at 2.70 MGy total absorbed dose · 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 7PPV · PDBe 7PPV · UniProt F9VPE5

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