Research workbench
Crystal structure of htpa reductase from neisseria meningitidis
Analyse Crystal structure of htpa reductase from neisseria meningitidis in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5UGJ
- Type
- protein
- Length
- 1,060 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- 4-hydroxy-tetrahydrodipicolinate reductase
- EC
- 1.17.1.8
- UniProt
- Q9K1F1
- Pockets
- 13 · best druggability 0.87
Structure
x-ray diffraction · 3 distinct chains · 35% helix, 27% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | 4-hydroxy-tetrahydrodipicolinate reductase (EC 1.17.1.8) | protein | 263 | 36% helix, 26% strand | Q9K1F1 |
| B | 4-hydroxy-tetrahydrodipicolinate reductase (EC 1.17.1.8) | protein | 265 | 35% helix, 27% strand | Q9K1F1 |
| C, D | 4-hydroxy-tetrahydrodipicolinate reductase (EC 1.17.1.8) | protein | 266 | 35% helix, 27% strand | Q9K1F1 |
Pockets
13 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 865 | 0.87 | 0.89 | 56 | empty |
| 2 | 1075 | 0.73 | 0.76 | 97 | empty |
| 3 | 882 | 0.72 | 0.77 | 77 | empty |
| 4 | 142 | 0.58 | 0.83 | 19 | empty |
| 5 | 180 | 0.56 | 0.80 | 22 | empty |
Interfaces
6 interfaces between chains.
- B–D · 1580 Ų buried · 34 hydrogen bonds · protein-protein
- A–C · 1565 Ų buried · 34 hydrogen bonds · protein-protein
- C–D · 1331 Ų buried · 24 hydrogen bonds · protein-protein
- A–B · 1235 Ų buried · 22 hydrogen bonds · protein-protein
- B–C · 346 Ų buried · 6 hydrogen bonds · protein-protein
Compared structures
- 5UGJ · Crystal structure of HTPA Reductase from neisseria meningitidis · the same entry in another collection · chain D against D, TM-score 1.00
- Q9K1F1 · AlphaFold monomer V2.0 prediction for 4-hydroxy- tetrahydrodipicolinate reductase (Q9K1F1) · a predicted model of the same protein · chain A against A, TM-score 0.98
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 Q9K1F1
- Elsewhere: RCSB PDB 5UGJ · PDBe 5UGJ · UniProt Q9K1F1
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