MolNFT v1 · #31453 · protein
Kinetics, stability, and structural changes in high resolution crystal structures of HIV-1 protease with drug resistant mutations L24I, I50V, and G73S
2AVM: “Kinetics, stability, and structural changes in high resolution crystal structures of HIV-1 protease with drug…”. X-ray diffraction. MolNFT v1 #31453 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 2AVM
- Type
- protein
- Length
- 199 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P04587
Structure
x-ray diffraction · 2 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 99 | — | P04587 |
| B | — | protein | 100 | — | P04587 |
Compared structures
- 2AVM · Kinetics, stability, and structural changes in high resolution crystal structures of… · 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 P04587
- Elsewhere: RCSB PDB 2AVM · PDBe 2AVM · UniProt P04587
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