MolNFT v1 · #132829 · protein
Pandda analysis group deposition -- endothiapepsin changed state model for fragment F2X-entry library H05A
5RCE: “Pandda analysis group deposition -- endothiapepsin changed state model for fragment F2X-entry library H05A”. X-ray diffraction, 1 ligand (RE4). MolNFT v1 #132829 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 5RCE
- Type
- protein
- Length
- 330 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P11838
- Ligands
- RE4
Structure
x-ray diffraction · 1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 330 | — | P11838 |
Ligands and binding sites
- RE4 · 6-methyl-N~4~-[(pyridin-3-yl)methyl]pyrimidine-2,4-diamine · ligand · 3 copies · chains A
- GOL · Glycerol · additive · 2 copies · chains A
- DMS · Dimethyl sulfoxide · additive · 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
- 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 5RCE · PDBe 5RCE · UniProt P11838
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