MolNFT v1 · #114892 · protein

Structural characterization of a newly identified component of alpha- carboxysomes: the aaa+ domain protein cso-cbbq

5C3C · CBBQ/NIRQ/NORQ domain protein: “Structural characterization of a newly identified component of alpha- carboxysomes: the aaa+ domain protein…”. X-ray diffraction, 1 ligand (ADP), 2 pockets (best druggability 0.81). MolNFT v1 #114892…

PDB: 5C3C
Type: protein
Length: 466 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: CBBQ/NIRQ/NORQ domain protein
UniProt: D0KZ75
Ligands: ADP
Pockets: 2 · best druggability 0.81

Structure

x-ray diffraction · 2 distinct chains · 46% helix, 14% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	CBBQ/NIRQ/NORQ domain protein	protein	231	45% helix, 14% strand	D0KZ75
B	CBBQ/NIRQ/NORQ domain protein	protein	235	48% helix, 14% strand	D0KZ75

Ligands and binding sites

ADP · Adenosine-5'-diphosphate · ligand · 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, 2 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	939	0.81	0.83	90	ADP
2	276	0.62	0.80	34	ADP

Interfaces

1 interface between chains.

A–B · 1435 Å² buried · 21 hydrogen bonds · protein-protein

Compared structures

5C3C · Structural characterization of a newly identified component of alpha-carboxysomes: The… · 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 D0KZ75
Elsewhere: RCSB PDB 5C3C · PDBe 5C3C · UniProt D0KZ75

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