MolNFT v1 · #183143 · protein
P1C-state of wild type human mitochondrial LONP1 protease with bound substrate protein in presence of ATP/ADP mix
7NG5: “P1C-state of wild type human mitochondrial LONP1 protease with bound substrate protein in presence of ATP/ADP…”. Electron microscopy, 3 ligands (ATP, ADP, MG). MolNFT v1 #183143 on GenesisL1: 3D structure, binding sites and pockets…
- PDB
- 7NG5
- Type
- protein
- Length
- 4,667 residues
- Chains
- 7
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P36776
- Ligands
- ATP, ADP, MG
Structure
electron microscopy · 2 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D, E, F | — | protein | 776 | — | P36776 |
| G | — | protein | 11 | — | — |
Ligands and binding sites
- ATP · Adenosine-5'-triphosphate · ligand · 5 copies · chains A, B, C, D, E, F
- ADP · Adenosine-5'-diphosphate · ligand · chains D
- MG · Magnesium ion · metal · 5 copies · chains A, B, C, E, F
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 7NG5 · P1c-state of wild type human mitochondrial LONP1 protease with bound substrate protein in… · the same entry in another collection · chain A 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 P36776
- Elsewhere: RCSB PDB 7NG5 · PDBe 7NG5 · UniProt P36776
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