MolNFT v1 · #164365 · protein
Crystal structure of the P235GK mutant of argbp from T. maritima
6SVF · Amino acid ABC transporter, periplasmic amino acid-binding…: “Crystal structure of the P235GK mutant of argbp from T. maritima”. X-ray diffraction, 1 ligand (ARG), 1 pocket (best druggability 0.34). MolNFT v1 #164365 on GenesisL1…
- PDB
- 6SVF
- Type
- protein
- Length
- 229 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Amino acid ABC transporter, periplasmic amino acid-binding protein
- UniProt
- Q9WZ62
- Ligands
- ARG
- Pockets
- 1 · best druggability 0.34
Structure
x-ray diffraction · 1 distinct chain · 38% helix, 24% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Amino acid ABC transporter, periplasmic amino acid-binding protein | protein | 229 | 38% helix, 24% strand | Q9WZ62 |
Ligands and binding sites
- ARG · Arginine · ligand · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 96 | 0.34 | 0.73 | 20 | empty |
Compared structures
- 6SVF · Crystal structure of the P235GK mutant of ArgBP from T. maritima · the same entry in another collection · 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 Q9WZ62
- Elsewhere: RCSB PDB 6SVF · PDBe 6SVF · UniProt Q9WZ62
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