4DWX
Crystal Structure of a Family GH-19 Chitinase from rye seeds
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000272 | biological_process | polysaccharide catabolic process |
| A | 0004568 | molecular_function | chitinase activity |
| A | 0005576 | cellular_component | extracellular region |
| A | 0005975 | biological_process | carbohydrate metabolic process |
| A | 0006032 | biological_process | chitin catabolic process |
| A | 0006952 | biological_process | defense response |
| A | 0008061 | molecular_function | chitin binding |
| A | 0008843 | molecular_function | endochitinase activity |
| A | 0016787 | molecular_function | hydrolase activity |
| A | 0016798 | molecular_function | hydrolase activity, acting on glycosyl bonds |
| A | 0016998 | biological_process | cell wall macromolecule catabolic process |
| A | 0031640 | biological_process | killing of cells of another organism |
| A | 0050832 | biological_process | defense response to fungus |
| B | 0000272 | biological_process | polysaccharide catabolic process |
| B | 0004568 | molecular_function | chitinase activity |
| B | 0005576 | cellular_component | extracellular region |
| B | 0005975 | biological_process | carbohydrate metabolic process |
| B | 0006032 | biological_process | chitin catabolic process |
| B | 0006952 | biological_process | defense response |
| B | 0008061 | molecular_function | chitin binding |
| B | 0008843 | molecular_function | endochitinase activity |
| B | 0016787 | molecular_function | hydrolase activity |
| B | 0016798 | molecular_function | hydrolase activity, acting on glycosyl bonds |
| B | 0016998 | biological_process | cell wall macromolecule catabolic process |
| B | 0031640 | biological_process | killing of cells of another organism |
| B | 0050832 | biological_process | defense response to fungus |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE MES A 301 |
| Chain | Residue |
| A | ILE117 |
| A | HOH625 |
| A | HOH634 |
| A | GLN118 |
| A | LEU119 |
| A | SER120 |
| A | ASN124 |
| A | PHE157 |
| A | ILE198 |
| A | HOH451 |
| A | HOH476 |
| site_id | AC2 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE SO4 A 302 |
| Chain | Residue |
| A | HIS8 |
| A | ASP12 |
| A | ARG18 |
| A | TYR29 |
| A | THR30 |
| A | TYR31 |
| A | ZN304 |
| A | HOH415 |
| A | HOH423 |
| A | HOH425 |
| A | HOH589 |
| B | ASP51 |
| B | HOH433 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE SO4 A 303 |
| Chain | Residue |
| A | SER100 |
| A | GLN102 |
| A | TRP103 |
| B | SER100 |
| B | GLN102 |
| B | TRP103 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN A 304 |
| Chain | Residue |
| A | HIS8 |
| A | ASP12 |
| A | SO4302 |
| B | ASP51 |
| site_id | AC5 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN A 305 |
| Chain | Residue |
| A | HIS17 |
| A | ASP20 |
| A | HOH590 |
| B | ASP232 |
| site_id | AC6 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE ZN A 306 |
| Chain | Residue |
| A | HIS121 |
| A | HOH428 |
| A | HOH479 |
| A | HOH501 |
| B | HIS206 |
| site_id | AC7 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE ZN A 307 |
| Chain | Residue |
| A | HIS206 |
| A | HOH532 |
| A | HOH554 |
| A | HOH618 |
| B | HIS121 |
| site_id | AC8 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE MES B 301 |
| Chain | Residue |
| B | ILE117 |
| B | GLN118 |
| B | LEU119 |
| B | SER120 |
| B | ASN124 |
| B | ILE198 |
| B | HOH440 |
| B | HOH452 |
| B | HOH490 |
| B | HOH580 |
| site_id | AC9 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE SO4 B 302 |
| Chain | Residue |
| B | HIS8 |
| B | ASP12 |
| B | ARG18 |
| B | THR30 |
| B | TYR31 |
| B | ZN303 |
| B | HOH516 |
| B | HOH685 |
| site_id | BC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN B 303 |
| Chain | Residue |
| B | HIS8 |
| B | ASP12 |
| B | SO4302 |
| B | HOH467 |
Functional Information from PROSITE/UniProt
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | Active site: {"description":"Proton donor","evidences":[{"source":"UniProtKB","id":"P29022","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | Site: {"description":"May be involved in substrate-binding","evidences":[{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"journal article","publicationDate":"1995","firstPage":"1076","lastPage":"1081","volume":"59","journal":"Biosci. Biotechnol. Biochem.","title":"Identification of the tryptophan residue located at the substrate-binding site of rye seed chitinase-c.","authors":["Yamagami T.","Funatsu G."]}}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | Site: {"description":"May be involved in substrate-binding","evidences":[{"source":"PubMed","id":"9532801","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
