Research workbench
Kinetic and structural characterization of a heterohexamer 4- oxalocrotonate tautomerase from chloroflexus aurantiacus J-10-fl: implications for functional and structural diversity in the tautomerase superfamily
Analyse Kinetic and structural characterization of a heterohexamer 4- oxalocrotonate… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3MB2
- Type
- protein
- Length
- 709 residues
- Chains
- 12
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- 4-oxalocrotonate tautomerase family enzyme - alpha subunit; 4-oxalocrotonate tautomerase…
- EC
- 5.3.2.2
- UniProt
- A9W9U6, A9W9V0
- Ligands
- SO4
- Pockets
- 16 · best druggability 0.77
Structure
x-ray diffraction · 6 distinct chains · 42% helix, 28% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, E, G | 4-oxalocrotonate tautomerase family enzyme - alpha subunit (EC 5.3.2.2) | protein | 61 | 41% helix, 34% strand | A9W9U6 |
| B, J | 4-oxalocrotonate tautomerase family enzyme - beta subunit (EC 5.3.2.2) | protein | 59 | 46% helix, 20% strand | A9W9V0 |
| C, K | 4-oxalocrotonate tautomerase family enzyme - alpha subunit (EC 5.3.2.2) | protein | 62 | 40% helix, 34% strand | A9W9U6 |
| D, H | 4-oxalocrotonate tautomerase family enzyme - beta subunit (EC 5.3.2.2) | protein | 58 | 45% helix, 21% strand | A9W9V0 |
| F, L | 4-oxalocrotonate tautomerase family enzyme - beta subunit (EC 5.3.2.2) | protein | 54 | 41% helix, 22% strand | A9W9V0 |
| I | 4-oxalocrotonate tautomerase family enzyme - alpha subunit (EC 5.3.2.2) | protein | 60 | 42% helix, 35% strand | A9W9U6 |
Ligands and binding sites
- SO4 · Sulfate ion · ion · 17 copies · chains A, D, C, I, B, E, G, F, K, H, J, L
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
16 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 661 | 0.77 | 0.82 | 90 | SO4 |
| 2 | 121 | 0.52 | 0.81 | 31 | empty |
| 3 | 99 | 0.48 | 0.80 | 14 | SO4 |
| 4 | 100 | 0.46 | 0.80 | 16 | SO4 |
| 5 | 72 | 0.46 | 0.83 | 22 | SO4 |
Interfaces
35 interfaces between chains.
- I–L · 1120 Ų buried · 16 hydrogen bonds · protein-protein
- H–K · 1116 Ų buried · 17 hydrogen bonds · protein-protein
- C–F · 1113 Ų buried · 15 hydrogen bonds · protein-protein
- A–D · 1089 Ų buried · 16 hydrogen bonds · protein-protein
- G–J · 1086 Ų buried · 17 hydrogen bonds · protein-protein
Compared structures
- 3MB2 · Kinetic and Structural Characterization of a Heterohexamer 4-Oxalocrotonate Tautomerase… · 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 A9W9U6
- Every structure of UniProt A9W9V0
- Elsewhere: RCSB PDB 3MB2 · PDBe 3MB2 · UniProt A9W9U6 · UniProt A9W9V0
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