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Crystal structure of udp-N-acetylglucosamine 1-carboxyvinyltransferase (mura) from stenotrophomonas maltophilia K279A
Analyse Crystal structure of udp-N-acetylglucosamine 1-carboxyvinyltransferase (mura)… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6WFM
- Type
- protein
- Length
- 833 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Udp-N-acetylglucosamine 1-carboxyvinyltransferase
- EC
- 2.5.1.7
- UniProt
- B2FRX1
- Pockets
- 4 · best druggability 0.72
Structure
x-ray diffraction · 2 distinct chains · 34% helix, 29% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Udp-N-acetylglucosamine 1-carboxyvinyltransferase (EC 2.5.1.7) | protein | 417 | 34% helix, 29% strand | B2FRX1 |
| B | Udp-N-acetylglucosamine 1-carboxyvinyltransferase (EC 2.5.1.7) | protein | 416 | 34% helix, 29% strand | B2FRX1 |
Pockets
4 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 544 | 0.72 | 0.80 | 73 | empty |
| 2 | 402 | 0.67 | 0.80 | 50 | empty |
| 3 | 316 | 0.56 | 0.76 | 48 | empty |
| 4 | 102 | 0.33 | 0.72 | 20 | empty |
Interfaces
1 interface between chains.
- A–B · 911 Ų buried · 10 hydrogen bonds · protein-protein
Compared structures
- 6WFM · Crystal structure of UDP-N-acetylglucosamine 1-carboxyvinyltransferase (murA) from… · the same entry in another collection · chain A against A, TM-score 1.00
- B2FRX1 · AlphaFold monomer V2.0 prediction for udp-N-acetylglucosamine 1-carboxyvinyltransferase… · a predicted model of the same protein · chain A against A, TM-score 0.93
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 B2FRX1
- Elsewhere: RCSB PDB 6WFM · PDBe 6WFM · UniProt B2FRX1
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