MolNFT v1 · #126496 · protein
Crystal structure of wild-type human prolidase with mn ions and pro ligand
5M4Q: “Crystal structure of wild-type human prolidase with mn ions and pro ligand”. X-ray diffraction, 2 ligands (MN, OH). MolNFT v1 #126496 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 5M4Q
- Type
- protein
- Length
- 964 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P12955
- Ligands
- MN, OH
Structure
x-ray diffraction · 2 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 485 | — | P12955 |
| B | — | protein | 479 | — | P12955 |
Ligands and binding sites
- MN · Manganese (II) ion · metal · 4 copies · chains A, B
- OH · Hydroxide ion · ion · 2 copies · chains A, B
- GOL · Glycerol · additive · 7 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 5M4Q · Crystal Structure of Wild-Type Human Prolidase with Mn ions and Pro ligand · the same entry in another collection · chain A against A, TM-score 1.00
- P12955 · AlphaFold monomer V2.0 prediction for xaa-pro dipeptidase (P12955) · a predicted model of the same protein · 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 P12955
- Elsewhere: RCSB PDB 5M4Q · PDBe 5M4Q · UniProt P12955
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