Research workbench
Phosphoglycerate mutase 1 H11 phosphorylated form complexed with KH1
Analyse Phosphoglycerate mutase 1 H11 phosphorylated form complexed with KH1 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5Y64
- Type
- protein
- Length
- 467 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P18669
- Ligands
- 8LF, CL
Structure
x-ray diffraction · 2 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| B | — | protein | 233 | — | P18669 |
| C | — | protein | 234 | — | P18669 |
Ligands and binding sites
- 8LF · ~{N}-[3,4-bis(oxidanyl)-9,10-bis(oxidanylidene) anthracen-2-yl]-4-methyl-benzenesulfonamide · ligand · chains C
- CL · Chloride ion · ion · chains B, C
- MES · 2-(N-morpholino)-ethanesulfonic acid · additive · chains C
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 5Y64 · Phosphoglycerate mutase 1 H11 phosphorylated form complexed with KH1 · the same entry in another collection · chain B against B, TM-score 1.00
- P18669 · AlphaFold monomer V2.0 prediction for phosphoglycerate mutase 1 (P18669) · a predicted model of the same protein · chain C against A, TM-score 0.98
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 P18669
- Elsewhere: RCSB PDB 5Y64 · PDBe 5Y64 · UniProt P18669
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