Research workbench
E. COLI (lacz) beta-galactosidase (ncs constrained monomer- orthorhombic)
Analyse E. COLI (lacz) beta-galactosidase (ncs constrained monomer- orthorhombic) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1F4A
- Type
- protein
- Length
- 4,084 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Beta-galactosidase
- EC
- 3.2.1.23
- UniProt
- P00722
- Ligands
- MG
- Pockets
- 20 · best druggability 0.81
Structure
x-ray diffraction · 1 distinct chain · 14% helix, 40% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D | Beta-galactosidase (EC 3.2.1.23) | protein | 1021 | 14% helix, 40% strand | P00722 |
Ligands and binding sites
- MG · Magnesium ion · metal · 8 copies · chains A, B, C, D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
20 pockets found on a 1 Å grid, 20 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 974 | 0.81 | 0.83 | 102 | empty |
| 2 | 836 | 0.80 | 0.83 | 79 | empty |
| 3 | 789 | 0.80 | 0.83 | 111 | empty |
| 4 | 464 | 0.78 | 0.86 | 70 | empty |
| 5 | 71 | 0.75 | 0.99 | 21 | empty |
Interfaces
6 interfaces between chains.
- B–C · 2400 Ų buried · 30 hydrogen bonds · protein-protein
- A–D · 2362 Ų buried · 30 hydrogen bonds · protein-protein
- A–B · 2023 Ų buried · 25 hydrogen bonds · protein-protein
- C–D · 2015 Ų buried · 25 hydrogen bonds · protein-protein
- A–C · 107 Ų buried · 3 hydrogen bonds · protein-protein
Compared structures
- 1F4A · E. COLI (lacz) beta-galactosidase (ncs constrained monomer-orthorhombic) · the same entry in another collection · chain D against D, TM-score 1.00
- P00722 · AlphaFold monomer V2.0 prediction for beta-galactosidase (P00722) · a predicted model of the same protein · 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 P00722
- Elsewhere: RCSB PDB 1F4A · PDBe 1F4A · UniProt P00722
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