Research workbench
X-ray structure of the bifunctional 6-hydroxymethyl-7,8- dihydroxypterin pyrophosphokinase dihydropteroate synthase from saccharomyces cerevisiae
Analyse X-ray structure of the bifunctional 6-hydroxymethyl-7,8- dihydroxypterin… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2BMB
- Type
- protein
- Length
- 513 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Folic acid synthesis protein FOL1
- EC
- 2.7.6.3, 6.3.2.12
- UniProt
- P53848
- Ligands
- PMM
- Pockets
- 9 · best druggability 0.70
Structure
x-ray diffraction · 1 distinct chain · 37% helix, 24% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Folic acid synthesis protein FOL1 (EC 2.7.6.3, 6.3.2.12) | protein | 513 | 37% helix, 24% strand | P53848 |
Ligands and binding sites
- PMM · Pterin-6-yl-methyl-monophosphate · ligand · 2 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
9 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 288 | 0.70 | 0.85 | 40 | PMM |
| 2 | 153 | 0.62 | 0.85 | 29 | empty |
| 3 | 117 | 0.50 | 0.80 | 22 | PMM |
| 4 | 154 | 0.49 | 0.78 | 25 | empty |
| 5 | 116 | 0.49 | 0.80 | 21 | empty |
Compared structures
- 2BMB · X-ray structure of the bifunctional 6-hydroxymethyl-7,8- dihydroxypterin… · the same entry in another collection · chain A against A, TM-score 1.00
- P53848 · AlphaFold monomer V2.0 prediction for folic acid synthesis protein FOL1 (P53848) · a predicted model of the same protein · chain A against A, TM-score 0.98
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 P53848
- Elsewhere: RCSB PDB 2BMB · PDBe 2BMB · UniProt P53848
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