MolNFT v1 · #61978 · protein

H. influenzae beta-carbonic anhydrase, variant D44N

3E1V · Carbonic anhydrase 2: “H. influenzae beta-carbonic anhydrase, variant D44N”. X-ray diffraction, 1 ligand (ZN), 4 pockets (best druggability 0.41). MolNFT v1 #61978 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 3E1V
Type: protein
Length: 364 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Carbonic anhydrase 2
EC: 4.2.1.1
UniProt: P45148
Ligands: ZN
Pockets: 4 · best druggability 0.41

Structure

x-ray diffraction · 1 distinct chain · 49% helix, 17% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Carbonic anhydrase 2 (EC 4.2.1.1)	protein	182	49% helix, 17% strand	P45148

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

4 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	70	0.41	0.80	23	empty
2	59	0.32	0.76	14	empty
3	64	0.30	0.74	16	empty
4	52	0.29	0.76	15	empty

Interfaces

1 interface between chains.

A–B · 1564 Å² buried · 19 hydrogen bonds · protein-protein

Compared structures

3E1V · H. influenzae beta-carbonic anhydrase, variant D44N · the same entry in another collection · chain A against A, TM-score 1.00
P45148 · AlphaFold monomer V2.0 prediction for carbonic anhydrase 2 (P45148) · a predicted model of the same protein · chain B against A, TM-score 0.98

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 P45148
Elsewhere: RCSB PDB 3E1V · PDBe 3E1V · UniProt P45148

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