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 | 0008061 | molecular_function | chitin binding |
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 | 0008061 | molecular_function | chitin binding |
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 | ACT_SITE: Proton donor => ECO:0000250|UniProtKB:P29022 |
Chain | Residue | Details |
A | GLU67 | |
B | GLU67 |
site_id | SWS_FT_FI2 |
Number of Residues | 2 |
Details | SITE: May be involved in substrate-binding => ECO:0000269|Ref.5 |
Chain | Residue | Details |
A | TRP72 | |
B | TRP72 |
site_id | SWS_FT_FI3 |
Number of Residues | 2 |
Details | SITE: May be involved in substrate-binding => ECO:0000269|PubMed:9532801 |
Chain | Residue | Details |
A | ASP95 | |
B | ASP95 |