Research workbench
High resolution structures of thermus aquaticus glyceraldehyde-3- phosphate dehydrogenase: role of 220'S loop motion in catalysis
Analyse High resolution structures of thermus aquaticus glyceraldehyde-3- phosphate… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2G82
- Type
- protein
- Length
- 2,640 residues
- Chains
- 8
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P00361
Structure
x-ray diffraction · 1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| O, P, Q, R, A, B, C, D | — | protein | 330 | — | P00361 |
Compared structures
- 2G82 · High Resolution Structures of Thermus aquaticus Glyceraldehyde-3-Phosphate Dehydrogenase… · the same entry in another collection · chain D against D, TM-score 1.00
- P00361 · AlphaFold monomer V2.0 prediction for glyceraldehyde-3-phosphate dehydrogenase (P00361) · a predicted model of the same protein · chain O 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 P00361
- Elsewhere: RCSB PDB 2G82 · PDBe 2G82 · UniProt P00361
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