MolNFT v1 · #70597 · protein

Crystal structure of human arginase I in complex with inhibitor N(OMEGA)-hydroxy-L-arginine (noha), 2.04A resolution

3LP7 · Arginase-1: “Crystal structure of human arginase I in complex with inhibitor N(OMEGA)-hydroxy-L-arginine (noha), 2.04A…”. X-ray diffraction, 2 ligands (HAR, MN), 4 pockets (best druggability 0.77). MolNFT v1 #70597 on GenesisL1: 3D…

PDB: 3LP7
Type: protein
Length: 626 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: HAR, MN
Pockets: 4 · best druggability 0.77

Structure

x-ray diffraction · 1 distinct chain · 42% helix, 15% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Arginase-1 (EC 3.5.3.1)	protein	313	42% helix, 15% strand	P05089

Ligands and binding sites

HAR · N-omega-hydroxy-L-arginine · ligand · 2 copies · chains A, B
MN · Manganese (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	0.77	0.79	97	HAR
2	88	0.43	0.80	19	HAR
3	52	0.33	0.78	15	empty
4	50	0.31	0.77	12	empty

Interfaces

1 interface between chains.

A–B · 466 Å² buried · 6 hydrogen bonds · protein-protein

Compared structures

3LP7 · Crystal structure of Human Arginase I in complex with inhibitor… · 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 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 P05089
Elsewhere: RCSB PDB 3LP7 · PDBe 3LP7 · UniProt P05089

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