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1.25 ångström resolution crystal structure of 4-hydroxythreonine-4- phosphate dehydrogenase from klebsiella pneumoniae.
Analyse 1.25 ångström resolution crystal structure of 4-hydroxythreonine-4- phosphate… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6E85
- Type
- protein
- Length
- 656 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- A0A1Y0PY16
- Ligands
- POP, NI, SO4, CL
Structure
x-ray diffraction · 2 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 331 | — | A0A1Y0PY16 |
| B | — | protein | 325 | — | A0A1Y0PY16 |
Ligands and binding sites
- POP · Pyrophosphate 2- · ligand · chains A
- NI · Nickel (II) ion · metal · 2 copies · chains A, B
- SO4 · Sulfate ion · ion · 4 copies · chains A, B
- CL · Chloride ion · ion · chains A
- FMT · Formic acid · additive · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 6E85 · 1.25 Angstrom Resolution Crystal Structure of 4-hydroxythreonine-4-phosphate… · 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 A0A1Y0PY16
- Elsewhere: RCSB PDB 6E85 · PDBe 6E85 · UniProt A0A1Y0PY16
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