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Crystal structure of recombinant human annexin IV
Analyse Crystal structure of recombinant human annexin IV in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2ZOC
- Type
- protein
- Length
- 637 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Annexin A4
- UniProt
- P09525
- Ligands
- CA
- Pockets
- 8 · best druggability 0.56
Structure
x-ray diffraction · 2 distinct chains · 71% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Annexin A4 | protein | 319 | 71% helix, 0% strand | P09525 |
| B | Annexin A4 | protein | 318 | 72% helix, 0% strand | P09525 |
Ligands and binding sites
- CA · Calcium ion · metal · 8 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
8 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 192 | 0.56 | 0.80 | 42 | empty |
| 2 | 110 | 0.55 | 0.84 | 23 | empty |
| 3 | 130 | 0.49 | 0.79 | 29 | empty |
| 4 | 95 | 0.39 | 0.76 | 18 | empty |
| 5 | 94 | 0.37 | 0.75 | 16 | empty |
Compared structures
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 P09525
- Elsewhere: RCSB PDB 2ZOC · PDBe 2ZOC · UniProt P09525
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