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Amino acid sequence and crystal structure of BAP1, a metalloproteinase from bothrops asper snake venom that exerts multiple tissue-damaging activities.
Analyse Amino acid sequence and crystal structure of BAP1, a metalloproteinase from… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1ND1
- Type
- protein
- Length
- 202 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- BAP1
- UniProt
- P83512
- Ligands
- ZN
- Pockets
- 1 · best druggability 0.46
Structure
x-ray diffraction · 1 distinct chain · 41% helix, 16% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | BAP1 | protein | 202 | 41% helix, 16% strand | P83512 |
Ligands and binding sites
- ZN · Zinc ion · metal · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 85 | 0.46 | 0.81 | 22 | empty |
Modifications
Observed in the structure: 3 disulfide, 1 modified (disulfide, cyclization).
Compared structures
- 1ND1 · Amino acid sequence and crystal structure of BaP1, a metalloproteinase from Bothrops… · the same entry in another collection · chain A against A, TM-score 1.00
- P83512 · AlphaFold monomer V2.0 prediction for snake venom metalloproteinase BAP1 (P83512) · a predicted model of the same protein · chain A against A, TM-score 0.96
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 P83512
- Elsewhere: RCSB PDB 1ND1 · PDBe 1ND1 · UniProt P83512
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