Research workbench
Studies of asymmetry in the three-dimensional structure of lobster D- glyceraldehyde-3-phosphate dehydrogenase
Analyse Studies of asymmetry in the three-dimensional structure of lobster D… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1GPD
- Type
- protein
- Length
- 666 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P00357
Structure
x-ray diffraction · 1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| G, R | — | protein | 333 | — | P00357 |
Compared structures
- 1GPD · Studies of asymmetry in the three-dimensional structure of lobster… · the same entry in another collection · chain G against G, TM-score 1.00
- P00357 · AlphaFold monomer V2.0 prediction for glyceraldehyde-3-phosphate dehydrogenase (P00357) · a predicted model of the same protein · chain G 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 P00357
- Elsewhere: RCSB PDB 1GPD · PDBe 1GPD · UniProt P00357
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