MolNFT v1 · #162819 · protein
Lysostaphin SH3B P4-G5 complex, synchrotron dataset
6RK4: “Lysostaphin SH3B P4-G5 complex, synchrotron dataset”. X-ray diffraction, 1 ligand (K5T). MolNFT v1 #162819 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 6RK4
- Type
- protein
- Length
- 93 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Lysostaphin
- EC
- 3.4.24.75
- UniProt
- P10547
- Ligands
- K5T
Structure
x-ray diffraction · 1 distinct chain · 0% helix, 57% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Lysostaphin (EC 3.4.24.75) | protein | 93 | 0% helix, 57% strand | P10547 |
Ligands and binding sites
- K5T · (2~{R})-2-[[(2~{S})-2-[[(4~{R})-5-azanyl-4-[[(2~{S})-2-azanylpropanoyl]amino]-5-oxidanylidene-pentanoyl]amino]-6-[2-[2-[2-[2-(2-azanylethanoylamino) ethanoylamino]ethanoylamino]ethanoylamino]ethanoylamin o]hexanoyl]amino]propanoic acid · ligand · chains A
- EDO · 1,2-ethanediol · additive · 2 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
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 P10547
- Elsewhere: RCSB PDB 6RK4 · PDBe 6RK4 · UniProt P10547
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