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Crystal structure of CO2+2-hai (pH 8.5)

Analyse Crystal structure of CO2+2-hai (pH 8.5) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3THE
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: BCN, CO
Pockets: 4 · best druggability 0.76

Structure

x-ray diffraction · 1 distinct chain · 41% helix, 16% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Arginase-1 (EC 3.5.3.1)	protein	314	41% helix, 16% strand	P05089

Ligands and binding sites

BCN · Bicine · ligand · 2 copies · chains A, B
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

4 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	984	0.76	0.78	80	BCN
2	95	0.44	0.80	21	BCN
3	67	0.39	0.79	17	empty
4	57	0.37	0.79	16	empty

Interfaces

1 interface between chains.

A–B · 450 Å² buried · 4 hydrogen bonds · protein-protein

Compared structures

3THE · Crystal structure of Co2+2-HAI (pH 8.5) · the same entry in another collection · chain B against B, TM-score 1.00
P05089 · AlphaFold monomer V2.0 prediction for arginase-1 (P05089) · a predicted model of the same protein · chain B 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 3THE · PDBe 3THE · UniProt P05089

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