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Crystal structure of dihydrofolate reductase (DHFR) from mycobacterium ulcerans AGY99 in complex with NADP and inhibitor sddc-0001914, tetragonal crystal from
Analyse Crystal structure of dihydrofolate reductase (DHFR) from mycobacterium ulcerans… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7KM7
- Type
- protein
- Length
- 158 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- A0PQG8
- Ligands
- NAP, WPD, BR
Structure
x-ray diffraction · 1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 158 | — | A0PQG8 |
Ligands and binding sites
- NAP · Nadp nicotinamide-adenine-dinucleotide phosphate · ligand · chains A
- WPD · (2S)-2-[(3-{3-[(2,4-diamino-6-ethylpyrimidin-5-yl) oxy]propoxy}phenyl)methyl]-3,3-difluoropropanoic acid · ligand · chains A
- BR · Bromide ion · ion · 2 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 7KM7 · Crystal Structure of Dihydrofolate reductase (DHFR) from Mycobacterium ulcerans Agy99 in… · 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 A0PQG8
- Elsewhere: RCSB PDB 7KM7 · PDBe 7KM7 · UniProt A0PQG8
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