Research workbench
Escherichia COLI murc
Analyse Escherichia COLI murc in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2F00
- Type
- protein
- Length
- 959 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Udp-N-acetylmuramate--L-alanine ligase
- EC
- 6.3.2.8
- UniProt
- P17952
- Ligands
- MG
- Pockets
- 10 · best druggability 0.77
Structure
x-ray diffraction · 2 distinct chains · 35% helix, 24% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Udp-N-acetylmuramate--L-alanine ligase (EC 6.3.2.8) | protein | 476 | 33% helix, 24% strand | P17952 |
| B | Udp-N-acetylmuramate--L-alanine ligase (EC 6.3.2.8) | protein | 483 | 37% helix, 24% strand | P17952 |
Ligands and binding sites
- 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
10 pockets found on a 1 Å grid, 7 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1200 | 0.77 | 0.79 | 116 | MG |
| 2 | 1117 | 0.76 | 0.79 | 124 | MG |
| 3 | 427 | 0.64 | 0.78 | 48 | empty |
| 4 | 81 | 0.58 | 0.87 | 28 | empty |
| 5 | 120 | 0.53 | 0.82 | 27 | empty |
Interfaces
1 interface between chains.
- A–B · 1272 Ų buried · 15 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 30 modified (engineered).
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 P17952
- Elsewhere: RCSB PDB 2F00 · PDBe 2F00 · UniProt P17952
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