MolNFT v1 · #132804 · protein
Pandda analysis group deposition -- endothiapepsin changed state model for fragment F2X-entry library B03A
5RBP: “Pandda analysis group deposition -- endothiapepsin changed state model for fragment F2X-entry library B03A”. X-ray diffraction, 2 ligands (SYG, NA). MolNFT v1 #132804 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 5RBP
- Type
- protein
- Length
- 330 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P11838
- Ligands
- SYG, NA
Structure
x-ray diffraction · 1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 330 | — | P11838 |
Ligands and binding sites
- SYG · 2-[(1~{S})-1-azanylpropyl]phenol · ligand · chains A
- NA · Sodium ion · metal
- DMS · Dimethyl sulfoxide · additive · 3 copies · chains A
- GOL · Glycerol · additive · 3 copies · chains A
- ACT · Acetate ion · additive · chains A
- PG4 · Tetraethylene glycol · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 5RBP · PanDDA analysis group deposition -- Endothiapepsin changed state model for fragment… · the same entry in another collection · chain A against A, TM-score 1.00
- P11838 · AlphaFold monomer V2.0 prediction for endothiapepsin (P11838) · 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 P11838
- Elsewhere: RCSB PDB 5RBP · PDBe 5RBP · UniProt P11838
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