MolNFT v1 · #136859 · protein
Phospho-ERK2 bound to AMP-pcp
5V60: “Phospho-ERK2 bound to AMP-pcp”. X-ray diffraction, 2 ligands (ACP, MG). MolNFT v1 #136859 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 5V60
- Type
- protein
- Length
- 349 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P28482
- Ligands
- ACP, MG
Structure
x-ray diffraction · 1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 349 | — | P28482 |
Ligands and binding sites
- ACP · Phosphomethylphosphonic acid adenylate ester · ligand · chains A
- MG · Magnesium ion · metal · 2 copies · chains A
- GOL · Glycerol · additive · 6 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 5V60 · Phospho-ERK2 bound to AMP-PCP · 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 P28482
- Elsewhere: RCSB PDB 5V60 · PDBe 5V60 · UniProt P28482
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