Research workbench
Candida glabrata dihydrofolate reductase complexed with NADPH and 5- [3-(2,5-DIMETHOXYPHENYL)PROP-1-yn-1-yl]-6-propylpyrimidine-2,4- diamine (UCP130B)
Analyse Candida glabrata dihydrofolate reductase complexed with NADPH and 5… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3QLZ
- Type
- protein
- Length
- 450 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- Q6FPH0
Structure
x-ray diffraction · 1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | — | protein | 225 | — | Q6FPH0 |
Compared structures
- 3QLZ · Candida glabrata dihydrofolate reductase complexed with NADPH and… · the same entry in another collection · 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 Q6FPH0
- Elsewhere: RCSB PDB 3QLZ · PDBe 3QLZ · UniProt Q6FPH0
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