MolNFT v1 · #22444 · protein

Arginase I-aoh complex

1T5F · Arginase 1: “Arginase I-aoh complex”. X-ray diffraction, 2 ligands (DHH, MN), 9 pockets (best druggability 0.81). MolNFT v1 #22444 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 1T5F
Type: protein
Length: 942 residues
Chains: 3
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Arginase 1
EC: 3.5.3.1
UniProt: P07824
Ligands: DHH, MN
Pockets: 9 · best druggability 0.81

Structure

x-ray diffraction · 1 distinct chain · 42% helix, 17% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B, C	Arginase 1 (EC 3.5.3.1)	protein	314	42% helix, 17% strand	P07824

Ligands and binding sites

DHH · (S)-2-amino-7,7-dihydroxyheptanoic acid · ligand · 3 copies · chains A, B, C
MN · Manganese (II) ion · metal · 6 copies · chains A, B, C

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

Pockets

9 pockets found on a 1 Å grid, 6 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	1158	0.81	0.82	100	empty
2	177	0.58	0.82	29	DHH
3	253	0.57	0.78	31	empty
4	180	0.57	0.81	26	DHH
5	168	0.56	0.81	26	DHH

Interfaces

3 interfaces between chains.

B–C · 998 Å² buried · 17 hydrogen bonds · protein-protein
A–C · 982 Å² buried · 16 hydrogen bonds · protein-protein
A–B · 957 Å² buried · 14 hydrogen bonds · protein-protein

Compared structures

1T5F · arginase I-AOH complex · the same entry in another collection · chain A against A, TM-score 1.00
P07824 · AlphaFold monomer V2.0 prediction for arginase-1 (P07824) · a predicted model of the same protein · chain C 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 P07824
Elsewhere: RCSB PDB 1T5F · PDBe 1T5F · UniProt P07824

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