MolNFT v1 · #153809 · protein

The structural basis of the beta-carbonic anhydrase cafc (L25G and L78G mutant) of the filamentous fungus aspergillus fumigatus

6JQD: “The structural basis of the beta-carbonic anhydrase cafc (L25G and L78G mutant) of the filamentous fungus…”. X-ray diffraction, 1 ligand (ZN), 3 pockets (best druggability 0.52). MolNFT v1 #153809 on GenesisL1: 3D structure, binding…

PDB: 6JQD
Type: protein
Length: 328 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Carbonic anhydrase
EC: 4.2.1.1
UniProt: Q4WPJ0
Ligands: ZN
Pockets: 3 · best druggability 0.52

Structure

x-ray diffraction · 1 distinct chain · 40% helix, 20% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Carbonic anhydrase (EC 4.2.1.1)	protein	164	40% helix, 20% strand	Q4WPJ0

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

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	79	0.52	0.85	21	ZN
2	83	0.50	0.83	20	empty
3	61	0.26	0.72	15	empty

Interfaces

1 interface between chains.

A–B · 3542 Å² buried · 52 hydrogen bonds · protein-protein

Compared structures

6JQD · The structural basis of the beta-carbonic anhydrase CafC (L25G and L78G mutant) of 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 Q4WPJ0
Elsewhere: RCSB PDB 6JQD · PDBe 6JQD · UniProt Q4WPJ0

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