Research workbench
Crystal structure of the periplasmic catecholate-siderophore binding protein vctp from vibrio cholerae
Analyse Crystal structure of the periplasmic catecholate-siderophore binding protein… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3TEF
- Type
- protein
- Length
- 279 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- IRON(III) ABC transporter, periplasmic iron-compound- binding protein
- UniProt
- Q9KMU2
- Pockets
- 2 · best druggability 0.46
Structure
x-ray diffraction · 1 distinct chain · 44% helix, 19% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | IRON(III) ABC transporter, periplasmic iron-compound- binding protein | protein | 279 | 44% helix, 19% strand | Q9KMU2 |
Pockets
2 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 113 | 0.46 | 0.79 | 21 | empty |
| 2 | 62 | 0.32 | 0.76 | 11 | empty |
Compared structures
- 3TEF · Crystal Structure of the Periplasmic Catecholate-Siderophore Binding Protein VctP from… · 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 Q9KMU2
- Elsewhere: RCSB PDB 3TEF · PDBe 3TEF · UniProt Q9KMU2
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