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Crystal structure of haemophilus influenzae mtsz at pH 7.0
Analyse Crystal structure of haemophilus influenzae mtsz at pH 7.0 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7L5I
- Type
- protein
- Length
- 763 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Trimethylamine-N-oxide reductase
- EC
- 1.7.2.3
- UniProt
- A0A2S9RK57
- Ligands
- MGD, MO, CL, O
- Pockets
- 4 · best druggability 0.85
Structure
x-ray diffraction · 1 distinct chain · 33% helix, 19% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Trimethylamine-N-oxide reductase (EC 1.7.2.3) | protein | 763 | 33% helix, 19% strand | A0A2S9RK57 |
Ligands and binding sites
- MGD · 2-amino-5,6-dimercapto-7-methyl-3,7,8A,9-tetrahydro-8-oxa-1,3,9,10-tetraaza-anthracen-4-one guanosine dinucleotide · ligand · 2 copies · chains A
- MO · Molybdenum atom · metal · chains A
- CL · Chloride ion · ion · chains A
- O · Oxygen atom · ion · chains A
- EPE · 4-(2-hydroxyethyl)-1-piperazine ethanesulfonic acid · additive · 3 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
4 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 745 | 0.85 | 0.89 | 104 | EPE, MGD, MO, O |
| 2 | 155 | 0.49 | 0.78 | 25 | empty |
| 3 | 173 | 0.47 | 0.76 | 21 | empty |
| 4 | 58 | 0.32 | 0.76 | 21 | empty |
Compared structures
- 7L5I · Crystal Structure of Haemophilus influenzae MtsZ at pH 7.0 · 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 A0A2S9RK57
- Elsewhere: RCSB PDB 7L5I · PDBe 7L5I · UniProt A0A2S9RK57
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