Research workbench
KD1 of human tfpi in complex with a synthetic peptide
Analyse KD1 of human tfpi in complex with a synthetic peptide in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4BQD
- Type
- protein
- Length
- 183 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Tissue factor pathway inhibitor (lipoprotein-associated coagulation inhibitor) variant…
- UniProt
- Q59EE5
- Ligands
- ACE
Structure
x-ray diffraction · 3 distinct chains · 20% helix, 26% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Tissue factor pathway inhibitor (lipoprotein-associated coagulation inhibitor) variant | protein | 78 | 15% helix, 31% strand | Q59EE5 |
| B | Tissue factor pathway inhibitor (lipoprotein-associated coagulation inhibitor) variant | protein | 65 | 18% helix, 25% strand | Q59EE5 |
| C, D | Peptide | protein | 20 | 40% helix, 15% strand | — |
Ligands and binding sites
- ACE · Acetyl group · ligand · 2 copies · chains A, C, B, D
- GOL · Glycerol · additive · 2 copies · chains B, D, A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Interfaces
4 interfaces between chains.
- A–C · 884 Ų buried · 11 hydrogen bonds · protein-protein
- B–D · 759 Ų buried · 11 hydrogen bonds · protein-protein
- A–D · 106 Ų buried · 2 hydrogen bonds · protein-protein
- A–B · 58 Ų buried · 0 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 6 disulfide, 2 modified (disulfide, nonstandard).
Compared structures
- 4BQD · KD1 of human TFPI in complex with a synthetic peptide · 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 Q59EE5
- Elsewhere: RCSB PDB 4BQD · PDBe 4BQD · UniProt Q59EE5
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.