MolNFT v1 · #79911 · protein

Crystal structure of unliganded CO2+2-hai (pH 7.0)

3TH7 · Arginase-1: “Crystal structure of unliganded CO2+2-hai (pH 7.0)”. X-ray diffraction, 1 ligand (CO), 2 pockets (best druggability 0.77). MolNFT v1 #79911 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 3TH7
Type: protein
Length: 628 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Arginase-1
EC: 3.5.3.1
UniProt: P05089
Ligands: CO
Pockets: 2 · best druggability 0.77

Structure

x-ray diffraction · 1 distinct chain · 41% helix, 17% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Arginase-1 (EC 3.5.3.1)	protein	314	41% helix, 17% strand	P05089

Ligands and binding sites

CO · Cobalt (II) ion · metal · 4 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, 1 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	977	0.77	0.80	92	empty
2	87	0.43	0.80	20	empty

Interfaces

1 interface between chains.

A–B · 422 Å² buried · 5 hydrogen bonds · protein-protein

Compared structures

3TH7 · Crystal structure of unliganded Co2+2-HAI (pH 7.0) · the same entry in another collection · chain A against A, TM-score 1.00
P05089 · AlphaFold monomer V2.0 prediction for arginase-1 (P05089) · a predicted model of the same protein · chain A against A, TM-score 0.99

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 P05089
Elsewhere: RCSB PDB 3TH7 · PDBe 3TH7 · UniProt P05089

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