Research workbench
Structural analysis of pneumocystis carinii and human DHFR complexes with NADPH and a series of five potent 5-(omega-CARBOXY(ALKYLOXY) PYRIDO[2,3-D]PYRIMIDINE derivatives
Analyse Structural analysis of pneumocystis carinii and human DHFR complexes with NADPH… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3NZ6
- Type
- protein
- Length
- 206 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P16184
Structure
x-ray diffraction · 1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| X | — | protein | 206 | — | P16184 |
Compared structures
- 3NZ6 · Structural Analysis of Pneumocystis carinii and Human DHFR Complexes with NADPH and a… · the same entry in another collection · chain X against X, TM-score 1.00
- P16184 · AlphaFold monomer V2.0 prediction for dihydrofolate reductase (P16184) · a predicted model of the same protein · chain X against A, TM-score 0.96
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 P16184
- Elsewhere: RCSB PDB 3NZ6 · PDBe 3NZ6 · UniProt P16184
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