4OIF
3D structure of Gan42B, a GH42 beta-galactosidase from G.
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0004565 | molecular_function | beta-galactosidase activity |
A | 0005975 | biological_process | carbohydrate metabolic process |
A | 0006012 | biological_process | galactose metabolic process |
A | 0009341 | cellular_component | beta-galactosidase complex |
A | 0016798 | molecular_function | hydrolase activity, acting on glycosyl bonds |
A | 0046872 | molecular_function | metal ion binding |
B | 0004565 | molecular_function | beta-galactosidase activity |
B | 0005975 | biological_process | carbohydrate metabolic process |
B | 0006012 | biological_process | galactose metabolic process |
B | 0009341 | cellular_component | beta-galactosidase complex |
B | 0016798 | molecular_function | hydrolase activity, acting on glycosyl bonds |
B | 0046872 | molecular_function | metal ion binding |
C | 0004565 | molecular_function | beta-galactosidase activity |
C | 0005975 | biological_process | carbohydrate metabolic process |
C | 0006012 | biological_process | galactose metabolic process |
C | 0009341 | cellular_component | beta-galactosidase complex |
C | 0016798 | molecular_function | hydrolase activity, acting on glycosyl bonds |
C | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE ZN A 701 |
Chain | Residue |
A | CYS124 |
A | CYS164 |
A | CYS166 |
A | CYS169 |
site_id | AC2 |
Number of Residues | 10 |
Details | BINDING SITE FOR RESIDUE GOL A 702 |
Chain | Residue |
A | HOH959 |
A | HOH1017 |
C | GLU532 |
C | THR533 |
C | GOL703 |
A | SER327 |
A | LEU328 |
A | LYS365 |
A | ASP379 |
A | HOH836 |
site_id | AC3 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE GOL A 703 |
Chain | Residue |
A | ARG120 |
A | ASN158 |
A | GLU159 |
A | GLU323 |
A | PHE361 |
A | GLU371 |
A | HOH816 |
A | HOH896 |
site_id | AC4 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE GOL A 704 |
Chain | Residue |
A | ARG120 |
A | GLU159 |
A | TRP331 |
A | HOH951 |
A | HOH1120 |
site_id | AC5 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE GOL A 705 |
Chain | Residue |
A | TRP518 |
A | HOH1037 |
B | GOL703 |
B | HOH934 |
B | HOH989 |
B | HOH1058 |
B | HOH1330 |
site_id | AC6 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE GOL A 706 |
Chain | Residue |
A | GLU452 |
A | ARG453 |
A | PHE622 |
A | VAL623 |
A | HIS625 |
A | HOH940 |
A | HOH949 |
site_id | AC7 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE GOL A 707 |
Chain | Residue |
A | ARG438 |
A | GLN441 |
A | THR442 |
A | GLN445 |
A | ARG598 |
A | HOH925 |
site_id | AC8 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE GOL A 708 |
Chain | Residue |
A | PRO411 |
A | ARG618 |
A | PRO619 |
A | HOH955 |
A | HOH1195 |
site_id | AC9 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE GOL A 709 |
Chain | Residue |
A | LYS42 |
A | HOH945 |
A | HOH1006 |
B | ALA142 |
B | GLU143 |
B | GLY146 |
B | ASP147 |
B | HOH879 |
site_id | BC1 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE ZN B 701 |
Chain | Residue |
B | CYS124 |
B | CYS164 |
B | CYS166 |
B | CYS169 |
site_id | BC2 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE GOL B 702 |
Chain | Residue |
B | ARG120 |
B | ASN158 |
B | GLU159 |
B | GLU323 |
B | PHE361 |
B | GLU371 |
B | HOH828 |
B | HOH1077 |
B | HOH1099 |
site_id | BC3 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE GOL B 703 |
Chain | Residue |
A | ILE506 |
A | GOL705 |
A | HOH863 |
A | HOH1003 |
B | PHE373 |
B | GOL704 |
B | HOH972 |
B | HOH989 |
site_id | BC4 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE GOL B 704 |
Chain | Residue |
A | THR533 |
B | SER327 |
B | LEU328 |
B | LYS365 |
B | VAL388 |
B | GOL703 |
B | HOH893 |
B | HOH1058 |
B | HOH1244 |
site_id | BC5 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE GOL B 705 |
Chain | Residue |
B | THR533 |
B | GOL707 |
B | HOH838 |
B | HOH936 |
B | HOH1011 |
C | SER327 |
C | LEU328 |
C | LYS365 |
C | ASP379 |
site_id | BC6 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE GOL B 706 |
Chain | Residue |
B | ARG438 |
B | GLN441 |
B | THR442 |
B | GLN445 |
B | ARG598 |
B | HOH1018 |
B | HOH1036 |
site_id | BC7 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE GOL B 707 |
Chain | Residue |
B | ILE506 |
B | GOL705 |
B | GOL708 |
B | HOH931 |
B | HOH945 |
B | HOH1022 |
C | PHE373 |
C | HOH893 |
site_id | BC8 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE GOL B 708 |
Chain | Residue |
B | GLY517 |
B | TRP518 |
B | GOL707 |
B | HOH936 |
B | HOH993 |
B | HOH1022 |
B | HOH1251 |
B | HOH1337 |
site_id | BC9 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE GOL B 709 |
Chain | Residue |
B | GLU452 |
B | ARG453 |
B | PHE622 |
B | VAL623 |
B | LYS624 |
B | HIS625 |
B | HOH1125 |
B | HOH1170 |
B | HOH1202 |
site_id | CC1 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE GOL B 710 |
Chain | Residue |
B | LEU43 |
B | GLN390 |
B | LYS397 |
B | HOH1174 |
C | ASP76 |
C | GOL705 |
site_id | CC2 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE GOL B 711 |
Chain | Residue |
B | PRO538 |
B | ARG539 |
B | HOH985 |
C | ASP293 |
C | TRP294 |
site_id | CC3 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE GOL B 712 |
Chain | Residue |
A | GLY214 |
B | GLN115 |
B | LEU116 |
B | GLY118 |
B | ASN122 |
B | HOH996 |
B | HOH1003 |
B | HOH1109 |
site_id | CC4 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE GOL B 713 |
Chain | Residue |
B | HIS464 |
B | ASP465 |
B | PHE466 |
B | ARG487 |
B | PHE491 |
site_id | CC5 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE ZN C 701 |
Chain | Residue |
C | CYS124 |
C | CYS164 |
C | CYS166 |
C | CYS169 |
site_id | CC6 |
Number of Residues | 10 |
Details | BINDING SITE FOR RESIDUE GOL C 702 |
Chain | Residue |
C | ARG120 |
C | ASN158 |
C | GLU159 |
C | ASP285 |
C | GLU323 |
C | PHE361 |
C | GLU371 |
C | HOH815 |
C | HOH996 |
C | HOH1193 |
site_id | CC7 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE GOL C 703 |
Chain | Residue |
A | PHE373 |
A | GOL702 |
A | HOH866 |
C | ILE506 |
C | HOH838 |
C | HOH1058 |
C | HOH1200 |
site_id | CC8 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE GOL C 704 |
Chain | Residue |
C | ASP465 |
C | PHE466 |
C | SER467 |
C | ARG487 |
site_id | CC9 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE GOL C 705 |
Chain | Residue |
B | GLN390 |
B | GLU394 |
B | LYS397 |
B | GOL710 |
C | ASP72 |
C | ARG144 |
C | HOH1190 |
site_id | DC1 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE GOL C 706 |
Chain | Residue |
B | ILE531 |
B | GLU532 |
C | ASP379 |
C | SER386 |
C | ARG387 |
C | VAL388 |
C | HOH896 |
Functional Information from PROSITE/UniProt
site_id | PS00018 |
Number of Residues | 13 |
Details | EF_HAND_1 EF-hand calcium-binding domain. DYNPDQWLDrpDI |
Chain | Residue | Details |
A | ASP21-ILE33 |