MolNFT v1 · #179975 · protein
Human ARGINASE1 complexed with inhibitor compound 3A
7KLK: “Human ARGINASE1 complexed with inhibitor compound 3A”. X-ray diffraction, 2 ligands (XFP, MN). MolNFT v1 #179975 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 7KLK
- Type
- protein
- Length
- 1,905 residues
- Chains
- 6
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P05089
- Ligands
- XFP, MN
Structure
x-ray diffraction · 5 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, C | — | protein | 317 | — | P05089 |
| B | — | protein | 318 | — | P05089 |
| D | — | protein | 318 | — | P05089 |
| E | — | protein | 319 | — | P05089 |
| F | — | protein | 316 | — | P05089 |
Ligands and binding sites
- XFP · 3-[(2~{S},3~{R})-2-carboxypiperidin-3-yl]propyl-$l^{3}-oxidanyl-bis(oxidanyl)boranuide · ligand · 6 copies · chains A, B, C, D, E, F
- MN · Manganese (II) ion · metal · 12 copies · chains A, B, C, D, E, F
- EDO · 1,2-ethanediol · additive · chains C, D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
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 7KLK · PDBe 7KLK · UniProt P05089
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