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Zn-bound domain 3 of CDCA1 in complex with carbon dioxide

Analyse Zn-bound domain 3 of CDCA1 in complex with carbon dioxide in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 7BF0
Type: protein
Length: 423 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Cadmium-specific carbonic anhydrase
UniProt: Q50EL4
Ligands: ZN, CO2, CL
Pockets: 1 · best druggability 0.54

Structure

x-ray diffraction · 2 distinct chains · 37% helix, 20% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Cadmium-specific carbonic anhydrase	protein	214	36% helix, 20% strand	Q50EL4
B	Cadmium-specific carbonic anhydrase	protein	209	37% helix, 20% strand	Q50EL4

Ligands and binding sites

ZN · Zinc ion · metal · 2 copies · chains A, B
CO2 · Carbon dioxide · ion · 2 copies · chains A, B
CL · Chloride ion · ion · 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	204	0.54	0.78	24	empty

Interfaces

1 interface between chains.

A–B · 551 Å² buried · 12 hydrogen bonds · protein-protein

Compared structures

7BF0 · Zn-bound domain 3 of CDCA1 in complex with carbon dioxide · 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 Q50EL4
Elsewhere: RCSB PDB 7BF0 · PDBe 7BF0 · UniProt Q50EL4

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