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2.2A crystal structure of co-CAO1

Analyse 2.2A crystal structure of co-CAO1 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6B86
Type: protein
Length: 1,988 residues
Chains: 4
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Carotenoid oxygenase 1
UniProt: Q7S860
Ligands: CO
Pockets: 20 · best druggability 0.88

Structure

x-ray diffraction · 1 distinct chain · 8% helix, 38% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B, C, D	Carotenoid oxygenase 1	protein	497	8% helix, 38% strand	Q7S860

Ligands and binding sites

CO · Cobalt (II) ion · metal · 4 copies · chains A, B, C, D

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

Pockets

20 pockets found on a 1 Å grid, 13 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	1074	0.88	0.89	140	empty
2	1072	0.84	0.85	123	empty
3	444	0.84	0.91	69	empty
4	417	0.84	0.91	70	empty
5	547	0.83	0.89	73	empty

Interfaces

4 interfaces between chains.

B–C · 1528 Å² buried · 34 hydrogen bonds · protein-protein
A–D · 1519 Å² buried · 35 hydrogen bonds · protein-protein
A–B · 384 Å² buried · 2 hydrogen bonds · protein-protein
C–D · 378 Å² buried · 2 hydrogen bonds · protein-protein

Compared structures

6B86 · 2.2A Crystal Structure of Co-CAO1 · 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 Q7S860
Elsewhere: RCSB PDB 6B86 · PDBe 6B86 · UniProt Q7S860

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