Research workbench
Mepa, inactive form without zn in P21
Analyse Mepa, inactive form without zn in P21 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1TZP
- Type
- protein
- Length
- 476 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Penicillin-insensitive murein endopeptidase
- EC
- 3.4.99.-
- UniProt
- P14007
- Ligands
- SO4
- Pockets
- 4 · best druggability 0.60
Structure
x-ray diffraction · 2 distinct chains · 28% helix, 18% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Penicillin-insensitive murein endopeptidase (EC 3.4.99.-) | protein | 240 | 28% helix, 18% strand | P14007 |
| B | Penicillin-insensitive murein endopeptidase (EC 3.4.99.-) | protein | 236 | 27% helix, 19% strand | P14007 |
Ligands and binding sites
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 | 116 | 0.60 | 0.86 | 20 | empty |
| 2 | 132 | 0.41 | 0.75 | 20 | empty |
| 3 | 112 | 0.38 | 0.74 | 22 | empty |
| 4 | 61 | 0.32 | 0.75 | 13 | empty |
Interfaces
1 interface between chains.
- A–B · 726 Ų buried · 3 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 6 disulfide (disulfide).
Compared structures
- 1TZP · MEPA, inactive form without ZN in P21 · 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 P14007
- Elsewhere: RCSB PDB 1TZP · PDBe 1TZP · UniProt P14007
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