Research workbench
Semet structure of a novel carbohydrate binding module from glycoside hydrolase family 9 (CEL9A) from ruminococcus flavefaciens fd-1
Analyse Semet structure of a novel carbohydrate binding module from glycoside hydrolase… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4V1K
- Type
- protein
- Length
- 131 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Carbohydrate binding module
- Ligands
- BGQ, CA
Structure
x-ray diffraction · 1 distinct chain · 12% helix, 53% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Carbohydrate binding module | protein | 131 | 12% helix, 53% strand | — |
Ligands and binding sites
- BGQ · 2-hydroxy butane-1,4-diol · ligand · chains A
- CA · Calcium ion · metal · 3 copies
- 2PE · Nonaethylene glycol · additive · chains A
- P6G · Hexaethylene glycol · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Modifications
Observed in the structure: 2 modified (engineered).
Compared structures
- 4V1K · SeMet structure of a novel carbohydrate binding module from glycoside hydrolase family 9… · 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
- Elsewhere: RCSB PDB 4V1K · PDBe 4V1K
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