MolNFT v1 · #173918 · protein

Zinc bound domain 3 of carbonic anhydrase from marine diatom thalassiosira weissflogii

7BEZ · Cadmium-specific carbonic anhydrase: “Zinc bound domain 3 of carbonic anhydrase from marine diatom thalassiosira weissflogii”. X-ray diffraction, 1 ligand (ZN), 2 pockets (best druggability 0.54). MolNFT v1 #173918 on GenesisL1: 3D…

PDB: 7BEZ
Type: protein
Length: 424 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Cadmium-specific carbonic anhydrase
UniProt: Q50EL4
Ligands: ZN
Pockets: 2 · best druggability 0.54

Structure

x-ray diffraction · 2 distinct chains · 36% 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	210	37% helix, 20% strand	Q50EL4

Ligands and binding sites

ZN · Zinc ion · metal · 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	69	0.54	0.86	16	empty
2	199	0.52	0.78	24	empty

Interfaces

1 interface between chains.

A–B · 565 Å² buried · 12 hydrogen bonds · protein-protein

Compared structures

7BEZ · Zinc bound domain 3 of carbonic anhydrase from marine diatom Thalassiosira weissflogii · 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 7BEZ · PDBe 7BEZ · UniProt Q50EL4

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