MolNFT v1 · #4129 · protein

X-ray structure of a beta-carbonic anhydrase from the red alga, porphyridium purpureum R-1

1DDZ: “X-ray structure of a beta-carbonic anhydrase from the red alga, porphyridium purpureum R-1”. X-ray diffraction, 1 ligand (ZN), 18 pockets (best druggability 0.78). MolNFT v1 #4129 on GenesisL1: 3D structure, binding sites and…

PDB: 1DDZ
Type: protein
Length: 962 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Carbonic anhydrase
EC: 4.2.1.1
UniProt: Q43060
Ligands: ZN
Pockets: 18 · best druggability 0.78

Structure

x-ray diffraction · 1 distinct chain · 46% helix, 13% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Carbonic anhydrase (EC 4.2.1.1)	protein	481	46% helix, 13% strand	Q43060

Ligands and binding sites

ZN · Zinc ion · metal · 4 copies · chains A, B

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

Pockets

18 pockets found on a 1 Å grid, 8 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	145	0.78	0.96	26	empty
2	83	0.77	0.99	24	empty
3	104	0.76	0.97	27	empty
4	77	0.74	0.97	26	empty
5	70	0.72	0.97	23	empty

Interfaces

1 interface between chains.

A–B · 4947 Å² buried · 87 hydrogen bonds · protein-protein

Compared structures

1DDZ · X-ray structure of a beta-carbonic anhydrase from the red alga, porphyridium purpureum R-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 Q43060
Elsewhere: RCSB PDB 1DDZ · PDBe 1DDZ · UniProt Q43060

GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.