Research workbench
Mobility of an HIV-1 integrase active site loop is correlated with catalytic activity
Analyse Mobility of an HIV-1 integrase active site loop is correlated with catalytic… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1B9F
- Type
- protein
- Length
- 151 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Protein (integrase)
- EC
- 2.7.7.49
- UniProt
- P12497
- Ligands
- SO4
Structure
x-ray diffraction · 1 distinct chain · 52% helix, 19% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Protein (integrase) (EC 2.7.7.49) | protein | 151 | 52% helix, 19% strand | P12497 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 1B9F · Mobility of an HIV-1 integrase active site loop is correlated with catalytic activity · 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 P12497
- Elsewhere: RCSB PDB 1B9F · PDBe 1B9F · UniProt P12497
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