Research workbench
Crystal structure of escherichia COLI GTPase BIPA/TYPA complexed with ppgpp
Analyse Crystal structure of escherichia COLI GTPase BIPA/TYPA complexed with ppgpp in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4ZCM
- Type
- protein
- Length
- 1,122 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- GTP-binding protein TYPA/BIPA
- UniProt
- P32132
- Ligands
- NCO, G4P, MG
- Pockets
- 20 · best druggability 0.74
Structure
x-ray diffraction · 1 distinct chain · 21% helix, 33% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | GTP-binding protein TYPA/BIPA | protein | 561 | 21% helix, 33% strand | P32132 |
Ligands and binding sites
- NCO · Cobalt hexammine(iii) · ligand · 4 copies · chains A, B
- G4P · Guanosine-5',3'-tetraphosphate · ligand · 2 copies · chains A, B
- MG · Magnesium ion · metal · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
20 pockets found on a 1 Å grid, 11 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 91 | 0.74 | 0.96 | 32 | empty |
| 2 | 703 | 0.74 | 0.80 | 72 | empty |
| 3 | 718 | 0.74 | 0.80 | 67 | empty |
| 4 | 289 | 0.70 | 0.84 | 34 | empty |
| 5 | 293 | 0.67 | 0.83 | 34 | empty |
Interfaces
1 interface between chains.
- A–B · 577 Ų buried · 2 hydrogen bonds · protein-protein
Compared structures
- 4ZCM · Crystal Structure of Escherichia coli GTPase BipA/TypA Complexed with ppGpp · the same entry in another collection · chain B against B, 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 P32132
- Elsewhere: RCSB PDB 4ZCM · PDBe 4ZCM · UniProt P32132
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