Research workbench
Crystal structure of the engineered mbp tem-1 fusion protein RG13, C2 space group
Analyse Crystal structure of the engineered mbp tem-1 fusion protein RG13, C2 space… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4DXC
- Type
- protein
- Length
- 624 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Maltose-binding periplasmic protein, beta-lactamase tem chimera
- EC
- 3.5.2.6
- UniProt
- P0AEX9, P62593
- Ligands
- ZN
- Pockets
- 5 · best druggability 0.78
Structure
x-ray diffraction · 1 distinct chain · 44% helix, 17% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Maltose-binding periplasmic protein, beta-lactamase tem chimera (EC 3.5.2.6) | protein | 624 | 44% helix, 17% strand | P0AEX9, P62593 |
Ligands and binding sites
- ZN · Zinc ion · metal · 2 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
5 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 870 | 0.78 | 0.81 | 72 | empty |
| 2 | 219 | 0.67 | 0.85 | 34 | empty |
| 3 | 370 | 0.58 | 0.75 | 28 | empty |
| 4 | 60 | 0.38 | 0.80 | 17 | empty |
| 5 | 59 | 0.37 | 0.79 | 19 | empty |
Modifications
Observed in the structure: 1 disulfide (disulfide).
Compared structures
- 4DXC · Crystal structure of the engineered MBP TEM-1 fusion protein RG13, C2 space group · the same entry in another collection · chain A against A, TM-score 1.00
- P62593 · AlphaFold monomer V2.0 prediction for beta-lactamase tem (P62593) · a predicted model of the same protein · chain A against A, TM-score 0.32
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 P0AEX9
- Every structure of UniProt P62593
- Elsewhere: RCSB PDB 4DXC · PDBe 4DXC · UniProt P0AEX9 · UniProt P62593
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