Research workbench
Structure of H200Q variant of homoprotocatechuate 2,3-dioxygenase from B.FUSCUM at 1.35 ang resolution
Analyse Structure of H200Q variant of homoprotocatechuate 2,3-dioxygenase from B.FUSCUM… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4Z6M
- Type
- protein
- Length
- 1,436 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Homoprotocatechuate 2,3-dioxygenase
- UniProt
- Q45135
- Ligands
- FE2, CA, CL
- Pockets
- 19 · best druggability 0.83
Structure
x-ray diffraction · 1 distinct chain · 18% helix, 35% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D | Homoprotocatechuate 2,3-dioxygenase | protein | 359 | 18% helix, 35% strand | Q45135 |
Ligands and binding sites
- FE2 · Fe (II) ion · metal · 4 copies · chains A, B, C, D
- CA · Calcium ion · metal · chains B
- CL · Chloride ion · ion · 4 copies · chains A, B, C, D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
19 pockets found on a 1 Å grid, 6 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 575 | 0.83 | 0.89 | 68 | empty |
| 2 | 607 | 0.83 | 0.88 | 66 | empty |
| 3 | 97 | 0.78 | 0.98 | 24 | empty |
| 4 | 100 | 0.77 | 0.98 | 23 | empty |
| 5 | 61 | 0.72 | 0.98 | 26 | empty |
Interfaces
6 interfaces between chains.
- B–D · 1686 Ų buried · 45 hydrogen bonds · protein-protein
- A–C · 1682 Ų buried · 45 hydrogen bonds · protein-protein
- C–D · 1671 Ų buried · 38 hydrogen bonds · protein-protein
- A–B · 1651 Ų buried · 34 hydrogen bonds · protein-protein
- B–C · 534 Ų buried · 2 hydrogen bonds · protein-protein
Compared structures
- 4Z6M · Structure of H200Q variant of Homoprotocatechuate 2,3-Dioxygenase from B.fuscum at 1.35… · 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 Q45135
- Elsewhere: RCSB PDB 4Z6M · PDBe 4Z6M · UniProt Q45135
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