MolNFT v1 · #50520 · protein
Structure of oppa complexed with lys-lys
2RKM · Oligo-peptide binding protein: “Structure of oppa complexed with lys-lys”. X-ray diffraction, 1 ligand (IUM), 3 pockets (best druggability 0.74). MolNFT v1 #50520 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 2RKM
- Type
- protein
- Length
- 519 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Oligo-peptide binding protein
- UniProt
- P06202
- Ligands
- IUM
- Pockets
- 3 · best druggability 0.74
Structure
x-ray diffraction · 1 distinct chain · 34% helix, 22% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Oligo-peptide binding protein | protein | 519 | 34% helix, 22% strand | P06202 |
Ligands and binding sites
- IUM · Uranyl (VI) ion · ligand · 8 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 80 | 0.74 | 0.97 | 29 | empty |
| 2 | 109 | 0.44 | 0.78 | 21 | empty |
| 3 | 71 | 0.30 | 0.74 | 18 | empty |
Modifications
Observed in the structure: 1 disulfide (disulfide).
Compared structures
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 P06202
- Elsewhere: RCSB PDB 2RKM · PDBe 2RKM · UniProt P06202
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.