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Crystal structure of ADAMTS4 (apo form)
Analyse Crystal structure of ADAMTS4 (apo form) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3B2Z
- Type
- protein
- Length
- 2,300 residues
- Chains
- 8
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Adamts-4
- EC
- 3.4.24.82
- UniProt
- O75173
- Ligands
- CA, ZN
- Pockets
- 16 · best druggability 0.82
Structure
x-ray diffraction · 7 distinct chains · 31% helix, 16% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Adamts-4 (EC 3.4.24.82) | protein | 290 | 30% helix, 17% strand | O75173 |
| B, D | Adamts-4 (EC 3.4.24.82) | protein | 287 | 33% helix, 17% strand | O75173 |
| C | Adamts-4 (EC 3.4.24.82) | protein | 289 | 30% helix, 16% strand | O75173 |
| E | Adamts-4 (EC 3.4.24.82) | protein | 282 | 29% helix, 18% strand | O75173 |
| F | Adamts-4 (EC 3.4.24.82) | protein | 293 | 31% helix, 17% strand | O75173 |
| G | Adamts-4 (EC 3.4.24.82) | protein | 291 | 32% helix, 15% strand | O75173 |
| H | Adamts-4 (EC 3.4.24.82) | protein | 281 | 31% helix, 16% strand | O75173 |
Ligands and binding sites
- CA · Calcium ion · metal · 16 copies · chains A, B, C, D, E, F, G, H
- ZN · Zinc ion · metal · 8 copies · chains A, B, C, D, E, F, G, H
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
16 pockets found on a 1 Å grid, 8 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1130 | 0.82 | 0.83 | 121 | empty |
| 2 | 1093 | 0.82 | 0.83 | 124 | empty |
| 3 | 978 | 0.79 | 0.81 | 118 | empty |
| 4 | 1057 | 0.79 | 0.80 | 119 | empty |
| 5 | 617 | 0.73 | 0.80 | 80 | empty |
Interfaces
12 interfaces between chains.
- B–F · 584 Ų buried · 4 hydrogen bonds · protein-protein
- A–B · 567 Ų buried · 2 hydrogen bonds · protein-protein
- A–E · 551 Ų buried · 4 hydrogen bonds · protein-protein
- C–D · 538 Ų buried · 4 hydrogen bonds · protein-protein
- D–G · 536 Ų buried · 3 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 64 disulfide (disulfide).
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 O75173
- Elsewhere: RCSB PDB 3B2Z · PDBe 3B2Z · UniProt O75173
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