MolNFT v1 · #153810 · protein

The structural basis of the beta-carbonic anhydrases cafd (wild type) of the filamentous fungus aspergillus fumigatus

6JQE: “The structural basis of the beta-carbonic anhydrases cafd (wild type) of the filamentous fungus aspergillus…”. X-ray diffraction, 1 ligand (ZN), 5 pockets (best druggability 0.45). MolNFT v1 #153810 on GenesisL1: 3D structure…

PDB: 6JQE
Type: protein
Length: 342 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Carbonic anhydrase
EC: 4.2.1.1
UniProt: A4DA31
Ligands: ZN
Pockets: 5 · best druggability 0.45

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	171	40% helix, 20% strand	A4DA31

Ligands and binding sites

ZN · Zinc ion · metal · 3 copies · chains A, B

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

5 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	132	0.45	0.77	27	empty
2	127	0.45	0.77	28	empty
3	84	0.36	0.76	17	empty
4	52	0.32	0.78	18	empty
5	61	0.29	0.74	18	empty

Interfaces

1 interface between chains.

A–B · 1338 Å² buried · 17 hydrogen bonds · protein-protein

Compared structures

6JQE · The structural basis of the beta-carbonic anhydrases CafD (wild type) of the filamentous… · 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 A4DA31
Elsewhere: RCSB PDB 6JQE · PDBe 6JQE · UniProt A4DA31

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