Research workbench
Three-dimensional structure of D-glyceraldehyde-3-phosphate dehydrogenase from the hyperthermophilic archaeon methanothermus fervidus
Analyse Three-dimensional structure of D-glyceraldehyde-3-phosphate dehydrogenase from… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1CF2
- Type
- protein
- Length
- 1,344 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P10618
Structure
x-ray diffraction · 1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| P, R, O, Q | — | protein | 336 | — | P10618 |
Compared structures
- 1CF2 · Three-dimensional structure of D-glyceraldehyde-3-phosphate dehydrogenase from the… · the same entry in another collection · chain P against P, TM-score 1.00
- P10618 · AlphaFold monomer V2.0 prediction for glyceraldehyde-3-phosphate dehydrogenase (P10618) · a predicted model of the same protein · chain P 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 P10618
- Elsewhere: RCSB PDB 1CF2 · PDBe 1CF2 · UniProt P10618
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