Research workbench
Thermostable GH159 glycoside hydrolase from caldicellulosiruptor at 1.7 a
Analyse Thermostable GH159 glycoside hydrolase from caldicellulosiruptor at 1.7 a in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7ZEI
- Type
- protein
- Length
- 1,857 residues
- Chains
- 6
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- E4QB49
- Ligands
- MG, CA
Structure
x-ray diffraction · 2 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, F | — | protein | 310 | — | E4QB49 |
| C, D, E | — | protein | 309 | — | E4QB49 |
Ligands and binding sites
- MG · Magnesium ion · metal · 6 copies · chains A, B, C, D, E, F
- CA · Calcium ion · metal · 6 copies · chains A, B, C, D, E, F
- GOL · Glycerol · additive · 16 copies · chains A, B, C, D, E, F
- MES · 2-(N-morpholino)-ethanesulfonic acid · additive · chains A
- TRS · 2-amino-2-hydroxymethyl-propane-1,3-diol · additive · chains B, E, F
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 7ZEI · Thermostable GH159 glycoside hydrolase from Caldicellulosiruptor at 1.7 A · 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 E4QB49
- Elsewhere: RCSB PDB 7ZEI · PDBe 7ZEI · UniProt E4QB49
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