Research workbench
Crystal structure of N-terminal domain 1 of vompd from bartonella quintana
Analyse Crystal structure of N-terminal domain 1 of vompd from bartonella quintana in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4LGO
- Type
- protein
- Length
- 353 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Vompd
- UniProt
- Q64HT0
Structure
x-ray diffraction · 3 distinct chains · 8% helix, 48% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Vompd | protein | 120 | 8% helix, 48% strand | Q64HT0 |
| B | Vompd | protein | 116 | 8% helix, 49% strand | Q64HT0 |
| C | Vompd | protein | 117 | 9% helix, 48% strand | Q64HT0 |
Ligands and binding sites
- EDO · 1,2-ethanediol · additive · 2 copies · chains B, C, A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Interfaces
3 interfaces between chains.
- A–C · 2745 Ų buried · 37 hydrogen bonds · protein-protein
- A–B · 2722 Ų buried · 39 hydrogen bonds · protein-protein
- B–C · 2636 Ų buried · 37 hydrogen bonds · protein-protein
Compared structures
- 4LGO · Crystal Structure of N-terminal domain 1 of VompD from Bartonella quintana · 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 Q64HT0
- Elsewhere: RCSB PDB 4LGO · PDBe 4LGO · UniProt Q64HT0
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