MolNFT v1 · #59126 · protein

Carbonic anhydrase from marine diatom thalassiosira weissflogii- cadmium bound domain 1 with acetate (CDCA1-R1)

3BOH · Cadmium-specific carbonic anhydrase: “Carbonic anhydrase from marine diatom thalassiosira weissflogii- cadmium bound domain 1 with acetate…”. X-ray diffraction, 1 ligand (CD), 1 pocket (best druggability 0.64). MolNFT v1 #59126 on…

PDB: 3BOH
Type: protein
Length: 426 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Cadmium-specific carbonic anhydrase
EC: 4.2.1.1
UniProt: Q50EL4
Ligands: CD
Pockets: 1 · best druggability 0.64

Structure

x-ray diffraction · 1 distinct chain · 36% helix, 20% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Cadmium-specific carbonic anhydrase (EC 4.2.1.1)	protein	213	36% helix, 20% strand	Q50EL4

Ligands and binding sites

CD · Cadmium ion · metal · 2 copies · chains A, B
ACT · Acetate ion · additive · 2 copies · chains A, B

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	385	0.64	0.79	50	empty

Interfaces

1 interface between chains.

A–B · 602 Å² buried · 1 hydrogen bond · protein-protein

Compared structures

3BOH · Carbonic anhydrase from marine diatom Thalassiosira weissflogii- cadmium bound domain 1… · 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 3BOH · PDBe 3BOH · UniProt Q50EL4

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