MolNFT v1 · #129622 · protein
A 3,6-anhydro-D-galactosidase produced by zobellia galactanivorans. this is an exo-lytic enzyme that hydrolyzes terminal 3,6-anhydro-D- galactose from the non-reducing end of carrageenan oligosaccharides.
5OPQ: “A 3,6-anhydro-D-galactosidase produced by zobellia galactanivorans. this is an exo-lytic enzyme that…”. X-ray diffraction, 1 ligand (CL). MolNFT v1 #129622 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 5OPQ
- Type
- protein
- Length
- 2,635 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- G0L004
- Ligands
- CL
Structure
x-ray diffraction · 2 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C | — | protein | 659 | — | G0L004 |
| D | — | protein | 658 | — | G0L004 |
Ligands and binding sites
- CL · Chloride ion · ion · 4 copies · chains A, B, C, D
- MPD · (4S)-2-methyl-2,4-pentanediol · additive · 5 copies · chains A, B, C, D
- TRS · 2-amino-2-hydroxymethyl-propane-1,3-diol · additive · 5 copies · chains A, B, C, D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 5OPQ · A 3,6-anhydro-D-galactosidase produced by Zobellia galactanivorans. This is an exo-lytic… · 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 G0L004
- Elsewhere: RCSB PDB 5OPQ · PDBe 5OPQ · UniProt G0L004
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