MolNFT v1 · #156697 · protein

Structure of helical carotenoid protein 2 from fremyella diplosiphon

6MCJ · Orange carotenoid-binding protein: “Structure of helical carotenoid protein 2 from fremyella diplosiphon”. X-ray diffraction, 2 ligands (45D, IOD), 1 pocket (best druggability 0.87). MolNFT v1 #156697 on GenesisL1: 3D structure…

PDB: 6MCJ
Type: protein
Length: 290 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Orange carotenoid-binding protein
UniProt: A0A0D6L0Q7
Ligands: 45D, IOD
Pockets: 1 · best druggability 0.87

Structure

x-ray diffraction · 1 distinct chain · 66% helix, 0% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Orange carotenoid-binding protein	protein	145	66% helix, 0% strand	A0A0D6L0Q7

Ligands and binding sites

45D · beta,beta-carotene-4,4'-dione · ligand · 2 copies · chains A, B
IOD · Iodide ion · ion · 8 copies · chains A, B
1PE · Pentaethylene glycol · additive · chains A

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

Pockets

1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	937	0.87	0.88	86	45D, 1PE, IOD

Interfaces

1 interface between chains.

A–B · 842 Å² buried · 26 hydrogen bonds · protein-protein

Compared structures

6MCJ · Structure of Helical Carotenoid Protein 2 from Fremyella diplosiphon · 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 A0A0D6L0Q7
Elsewhere: RCSB PDB 6MCJ · PDBe 6MCJ · UniProt A0A0D6L0Q7

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