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Structure of kdnase from trichophyton rubrum in complex with 2,3- didehydro-2,3-dideoxy-D-glycero-D-galacto-nonulosonic acid.
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- PDB
- 7P1S
- Type
- protein
- Length
- 1,523 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- A0A178EUH2
- Ligands
- KFN, NA
Structure
x-ray diffraction · 2 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 380 | — | A0A178EUH2 |
| B, C, D | — | protein | 381 | — | A0A178EUH2 |
Ligands and binding sites
- KFN · 2,6-anhydro-3-deoxy-D-glycero-D-galacto-non-2-enonic acid · ligand · 4 copies · chains A, B, C, D
- NA · Sodium ion · metal · 4 copies · chains A, B, C, D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 7P1S · Structure of KDNase from Trichophyton Rubrum in complex with… · the same entry in another collection · chain B against B, 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 A0A178EUH2
- Elsewhere: RCSB PDB 7P1S · PDBe 7P1S · UniProt A0A178EUH2
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