2YBU
Crystal structure of human acidic chitinase in complex with bisdionin F
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0004553 | molecular_function | hydrolase activity, hydrolyzing O-glycosyl compounds |
A | 0005975 | biological_process | carbohydrate metabolic process |
A | 0008061 | molecular_function | chitin binding |
B | 0004553 | molecular_function | hydrolase activity, hydrolyzing O-glycosyl compounds |
B | 0005975 | biological_process | carbohydrate metabolic process |
B | 0008061 | molecular_function | chitin binding |
C | 0004553 | molecular_function | hydrolase activity, hydrolyzing O-glycosyl compounds |
C | 0005975 | biological_process | carbohydrate metabolic process |
C | 0008061 | molecular_function | chitin binding |
D | 0004553 | molecular_function | hydrolase activity, hydrolyzing O-glycosyl compounds |
D | 0005975 | biological_process | carbohydrate metabolic process |
D | 0008061 | molecular_function | chitin binding |
E | 0004553 | molecular_function | hydrolase activity, hydrolyzing O-glycosyl compounds |
E | 0005975 | biological_process | carbohydrate metabolic process |
E | 0008061 | molecular_function | chitin binding |
F | 0004553 | molecular_function | hydrolase activity, hydrolyzing O-glycosyl compounds |
F | 0005975 | biological_process | carbohydrate metabolic process |
F | 0008061 | molecular_function | chitin binding |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE GOL A 1397 |
Chain | Residue |
A | TRP31 |
A | ARG35 |
A | GLU297 |
A | TRP360 |
A | CX91398 |
A | HOH2008 |
site_id | AC2 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE GOL B 1397 |
Chain | Residue |
B | ILE300 |
B | TRP360 |
B | CX91398 |
B | HOH2211 |
B | TRP31 |
B | ARG35 |
B | GLU297 |
site_id | AC3 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE GOL C 1397 |
Chain | Residue |
C | TRP31 |
C | ARG35 |
C | TRP360 |
C | CX91398 |
C | HOH2197 |
site_id | AC4 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE GOL D 1397 |
Chain | Residue |
D | TRP31 |
D | ARG35 |
D | GLU297 |
D | TRP360 |
D | CX91398 |
D | HOH2158 |
site_id | AC5 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE GOL E 1397 |
Chain | Residue |
E | TRP31 |
E | ARG35 |
E | GLU297 |
E | TRP360 |
E | LEU364 |
E | CX91398 |
E | HOH2168 |
site_id | AC6 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE GOL F 1397 |
Chain | Residue |
F | TRP31 |
F | ARG35 |
F | GLU297 |
F | ILE300 |
F | TRP360 |
F | LEU364 |
F | CX91398 |
F | HOH2113 |
site_id | AC7 |
Number of Residues | 15 |
Details | BINDING SITE FOR RESIDUE CX9 A 1398 |
Chain | Residue |
A | TRP31 |
A | PHE58 |
A | GLY98 |
A | TRP99 |
A | ASN100 |
A | ASP138 |
A | GLU140 |
A | MET210 |
A | TYR212 |
A | TYR267 |
A | TRP360 |
A | GOL1397 |
A | HOH2057 |
A | HOH2129 |
A | HOH2213 |
site_id | AC8 |
Number of Residues | 14 |
Details | BINDING SITE FOR RESIDUE CX9 B 1398 |
Chain | Residue |
B | TRP31 |
B | PHE58 |
B | GLY98 |
B | TRP99 |
B | ASN100 |
B | ASP138 |
B | GLU140 |
B | MET210 |
B | TYR212 |
B | TYR267 |
B | TRP360 |
B | GOL1397 |
B | HOH2059 |
B | HOH2220 |
site_id | AC9 |
Number of Residues | 13 |
Details | BINDING SITE FOR RESIDUE CX9 C 1398 |
Chain | Residue |
C | TRP31 |
C | PHE58 |
C | GLY98 |
C | TRP99 |
C | ASN100 |
C | ASP138 |
C | GLU140 |
C | MET210 |
C | TYR212 |
C | TYR267 |
C | TRP360 |
C | GOL1397 |
C | HOH2198 |
site_id | BC1 |
Number of Residues | 15 |
Details | BINDING SITE FOR RESIDUE CX9 D 1398 |
Chain | Residue |
D | TRP31 |
D | PHE58 |
D | GLY98 |
D | TRP99 |
D | ASN100 |
D | ASP138 |
D | GLU140 |
D | MET210 |
D | TYR212 |
D | TYR267 |
D | TRP360 |
D | GOL1397 |
D | HOH2042 |
D | HOH2170 |
D | HOH2171 |
site_id | BC2 |
Number of Residues | 13 |
Details | BINDING SITE FOR RESIDUE CX9 E 1398 |
Chain | Residue |
E | TRP99 |
E | ASN100 |
E | ASP138 |
E | GLU140 |
E | MET210 |
E | TYR212 |
E | TYR267 |
E | TRP360 |
E | GOL1397 |
E | HOH2193 |
E | TRP31 |
E | PHE58 |
E | GLY98 |
site_id | BC3 |
Number of Residues | 14 |
Details | BINDING SITE FOR RESIDUE CX9 F 1398 |
Chain | Residue |
F | TRP31 |
F | PHE58 |
F | GLY98 |
F | TRP99 |
F | ASN100 |
F | ASP138 |
F | GLU140 |
F | MET210 |
F | TYR212 |
F | TYR267 |
F | TRP360 |
F | GOL1397 |
F | HOH2090 |
F | HOH2123 |
site_id | BC4 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE CX9 A 1399 |
Chain | Residue |
A | TRP99 |
A | TRP218 |
A | HOH2086 |
site_id | BC5 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE CX9 B 1399 |
Chain | Residue |
B | TRP99 |
B | TRP218 |
site_id | BC6 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE CX9 C 1399 |
Chain | Residue |
C | TRP99 |
C | TRP218 |
C | HOH2069 |
C | HOH2199 |
site_id | BC7 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE CX9 D 1399 |
Chain | Residue |
A | GLN62 |
D | TRP99 |
D | TRP218 |
site_id | BC8 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE CX9 E 1399 |
Chain | Residue |
E | TRP99 |
E | TRP218 |
site_id | BC9 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE CX9 F 1399 |
Chain | Residue |
F | TRP99 |
F | TRP218 |
Functional Information from PROSITE/UniProt
site_id | PS01095 |
Number of Residues | 9 |
Details | GH18_1 Glycosyl hydrolases family 18 (GH18) active site signature. FDGLDFDwE |
Chain | Residue | Details |
A | PHE132-GLU140 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 6 |
Details | ACT_SITE: Proton donor => ECO:0000255|PROSITE-ProRule:PRU01258 |
Chain | Residue | Details |
A | GLU140 | |
B | GLU140 | |
C | GLU140 | |
D | GLU140 | |
E | GLU140 | |
F | GLU140 |
site_id | SWS_FT_FI2 |
Number of Residues | 30 |
Details | BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU01258 |
Chain | Residue | Details |
A | GLU70 | |
B | TRP360 | |
C | GLU70 | |
C | GLY97 | |
C | TYR141 | |
C | MET210 | |
C | TRP360 | |
D | GLU70 | |
D | GLY97 | |
D | TYR141 | |
D | MET210 | |
A | GLY97 | |
D | TRP360 | |
E | GLU70 | |
E | GLY97 | |
E | TYR141 | |
E | MET210 | |
E | TRP360 | |
F | GLU70 | |
F | GLY97 | |
F | TYR141 | |
F | MET210 | |
A | TYR141 | |
F | TRP360 | |
A | MET210 | |
A | TRP360 | |
B | GLU70 | |
B | GLY97 | |
B | TYR141 | |
B | MET210 |