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Crystal structure of the heterotetrameric complex of glucd and glucdrp from E. COLI K-12 MG1655 (efi target efi-506058)
Analyse Crystal structure of the heterotetrameric complex of glucd and glucdrp from E.… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4GYP
- Type
- protein
- Length
- 1,754 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P0AES2, Q46915
Structure
x-ray diffraction · 4 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 444 | — | P0AES2 |
| B | — | protein | 443 | — | P0AES2 |
| C | — | protein | 427 | — | Q46915 |
| D | — | protein | 440 | — | Q46915 |
Compared structures
- 4GYP · Crystal structure of the heterotetrameric complex of GlucD and GlucDRP from E. coli K-12… · the same entry in another collection · chain D against D, TM-score 1.00
- P0AES2 · AlphaFold monomer V2.0 prediction for glucarate dehydratase (P0AES2) · a predicted model of the same protein · chain B against A, TM-score 1.00
- Q46915 · AlphaFold monomer V2.0 prediction for glucarate dehydratase-related protein (Q46915) · a predicted model of the same protein · chain D 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 P0AES2
- Every structure of UniProt Q46915
- Elsewhere: RCSB PDB 4GYP · PDBe 4GYP · UniProt P0AES2 · UniProt Q46915
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