MolNFT v1 · #107980 · protein
The structure of the C-terminal yada-like domain of BPSL2063 from burkholderia pseudomallei
4USX · Trimeric autotransporter adhesin: “The structure of the C-terminal yada-like domain of BPSL2063 from burkholderia pseudomallei”. X-ray diffraction, 1 ligand (MG). MolNFT v1 #107980 on GenesisL1: 3D structure, binding sites and…
- PDB
- 4USX
- Type
- protein
- Length
- 633 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Trimeric autotransporter adhesin
- UniProt
- Q63TA4
- Ligands
- MG
Structure
x-ray diffraction · 3 distinct chains · 22% helix, 26% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Trimeric autotransporter adhesin | protein | 208 | 22% helix, 26% strand | Q63TA4 |
| B | Trimeric autotransporter adhesin | protein | 211 | 22% helix, 25% strand | Q63TA4 |
| C | Trimeric autotransporter adhesin | protein | 214 | 21% helix, 26% strand | Q63TA4 |
Ligands and binding sites
- MG · Magnesium ion · metal · 7 copies · chains A, C, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Interfaces
3 interfaces between chains.
- A–B · 4451 Ų buried · 76 hydrogen bonds · protein-protein
- A–C · 4440 Ų buried · 77 hydrogen bonds · protein-protein
- B–C · 4429 Ų buried · 74 hydrogen bonds · protein-protein
Compared structures
- 4USX · The Structure of the C-terminal YadA-like domain of BPSL2063 from Burkholderia… · 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 Q63TA4
- Elsewhere: RCSB PDB 4USX · PDBe 4USX · UniProt Q63TA4
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.