Research workbench
Mazf from S. aureus crystal form I, P212121, 2.1 a
Analyse Mazf from S. aureus crystal form I, P212121, 2.1 a in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4MZM
- Type
- protein
- Length
- 446 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- MRNA interferase mazf
- EC
- 3.1.-.-
- UniProt
- Q7A4G9
- Pockets
- 5 · best druggability 0.73
Structure
x-ray diffraction · 4 distinct chains · 21% helix, 38% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | MRNA interferase mazf (EC 3.1.-.-) | protein | 115 | 20% helix, 38% strand | Q7A4G9 |
| B | MRNA interferase mazf (EC 3.1.-.-) | protein | 109 | 21% helix, 39% strand | Q7A4G9 |
| C | MRNA interferase mazf (EC 3.1.-.-) | protein | 108 | 21% helix, 38% strand | Q7A4G9 |
| D | MRNA interferase mazf (EC 3.1.-.-) | protein | 114 | 20% helix, 39% strand | Q7A4G9 |
Pockets
5 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 656 | 0.73 | 0.80 | 73 | empty |
| 2 | 325 | 0.59 | 0.77 | 43 | empty |
| 3 | 56 | 0.40 | 0.81 | 17 | empty |
| 4 | 68 | 0.36 | 0.77 | 16 | empty |
| 5 | 71 | 0.28 | 0.72 | 15 | empty |
Interfaces
6 interfaces between chains.
- A–B · 1309 Ų buried · 31 hydrogen bonds · protein-protein
- C–D · 1283 Ų buried · 34 hydrogen bonds · protein-protein
- A–D · 245 Ų buried · 2 hydrogen bonds · protein-protein
- A–C · 235 Ų buried · 0 hydrogen bonds · protein-protein
- B–C · 162 Ų buried · 2 hydrogen bonds · protein-protein
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 Q7A4G9
- Elsewhere: RCSB PDB 4MZM · PDBe 4MZM · UniProt Q7A4G9
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