2XN0
Structure of alpha-galactosidase from Lactobacillus acidophilus NCFM, PtCl4 derivative
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004553 | molecular_function | hydrolase activity, hydrolyzing O-glycosyl compounds |
| A | 0004557 | molecular_function | alpha-galactosidase activity |
| A | 0005975 | biological_process | carbohydrate metabolic process |
| A | 0016052 | biological_process | carbohydrate catabolic process |
| A | 0016787 | molecular_function | hydrolase activity |
| A | 0016798 | molecular_function | hydrolase activity, acting on glycosyl bonds |
| A | 0051289 | biological_process | protein homotetramerization |
| A | 1901545 | biological_process | response to raffinose |
| B | 0004553 | molecular_function | hydrolase activity, hydrolyzing O-glycosyl compounds |
| B | 0004557 | molecular_function | alpha-galactosidase activity |
| B | 0005975 | biological_process | carbohydrate metabolic process |
| B | 0016052 | biological_process | carbohydrate catabolic process |
| B | 0016787 | molecular_function | hydrolase activity |
| B | 0016798 | molecular_function | hydrolase activity, acting on glycosyl bonds |
| B | 0051289 | biological_process | protein homotetramerization |
| B | 1901545 | biological_process | response to raffinose |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE PT A 1733 |
| Chain | Residue |
| A | LYS561 |
| A | HIS674 |
| A | HOH2410 |
| site_id | AC2 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE PT A 1734 |
| Chain | Residue |
| A | HIS709 |
| A | PT1735 |
| A | PT1737 |
| site_id | AC3 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE PT A 1735 |
| Chain | Residue |
| A | HIS709 |
| A | PT1734 |
| A | PT1737 |
| site_id | AC4 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE PT A 1736 |
| Chain | Residue |
| A | MET708 |
| A | HOH2418 |
| site_id | AC5 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE PT A 1737 |
| Chain | Residue |
| A | MET708 |
| A | HIS709 |
| A | PT1734 |
| A | PT1735 |
| site_id | AC6 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE PT A 1738 |
| Chain | Residue |
| A | MET247 |
| site_id | AC7 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE PT A 1739 |
| Chain | Residue |
| A | MET725 |
| site_id | AC8 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE PT A 1740 |
| Chain | Residue |
| A | MET672 |
| A | MET672 |
| A | HOH2165 |
| A | HOH2165 |
| site_id | AC9 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE PT B 1733 |
| Chain | Residue |
| B | MET672 |
| B | MET672 |
| site_id | BC1 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE PT B 1734 |
| Chain | Residue |
| B | HIS674 |
| site_id | BC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE PT B 1735 |
| Chain | Residue |
| A | HOH2219 |
| B | HIS709 |
| B | PT1736 |
| B | PT1738 |
| site_id | BC3 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE PT B 1736 |
| Chain | Residue |
| B | HIS709 |
| B | PT1735 |
| B | PT1738 |
| site_id | BC4 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE PT B 1737 |
| Chain | Residue |
| B | MET708 |
| site_id | BC5 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE PT B 1738 |
| Chain | Residue |
| B | MET708 |
| B | HIS709 |
| B | PT1735 |
| B | PT1736 |
| site_id | BC6 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE PT B 1739 |
| Chain | Residue |
| B | MET247 |
| B | HOH2180 |
| site_id | BC7 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE PT B 1740 |
| Chain | Residue |
| B | MET725 |
| site_id | BC8 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE GOL A 1741 |
| Chain | Residue |
| A | ASP370 |
| A | LYS480 |
| A | ASP482 |
| A | ASN484 |
| A | CYS530 |
| A | GLY533 |
| A | ASP552 |
| A | GOL1744 |
| A | HOH2452 |
| site_id | BC9 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE GOL A 1742 |
| Chain | Residue |
| A | SER146 |
| A | LYS147 |
| A | GLY173 |
| A | GLU174 |
| A | GLU175 |
| site_id | CC1 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE GOL A 1743 |
| Chain | Residue |
| A | GLY84 |
| A | GLU85 |
| A | MET86 |
| A | ASP87 |
| A | PHE88 |
| A | HOH2065 |
| B | TYR282 |
| B | LEU487 |
| B | SER488 |
| B | TYR504 |
| site_id | CC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE GOL A 1744 |
| Chain | Residue |
| A | ARG447 |
| A | ASN484 |
| A | GOL1741 |
| A | HOH2453 |
| B | PHE59 |
| site_id | CC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE GOL A 1745 |
| Chain | Residue |
| A | HIS320 |
| A | GLU321 |
| A | PHE638 |
| A | HOH2223 |
| A | HOH2345 |
| site_id | CC4 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE GOL B 1741 |
| Chain | Residue |
| B | TRP340 |
| B | ASP370 |
| B | LYS480 |
| B | ASP482 |
| B | ASN484 |
| B | CYS530 |
| B | TRP549 |
| B | ASP552 |
| B | GOL1744 |
| B | HOH2231 |
| site_id | CC5 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE GOL B 1742 |
| Chain | Residue |
| B | SER146 |
| B | GLY173 |
| B | GLU174 |
| B | GLU175 |
| site_id | CC6 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE GOL B 1743 |
| Chain | Residue |
| A | TYR224 |
| A | TYR282 |
| A | LEU487 |
| A | SER488 |
| A | TYR504 |
| B | ALA83 |
| B | GLY84 |
| B | GLU85 |
| B | MET86 |
| B | PHE88 |
| site_id | CC7 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE GOL B 1744 |
| Chain | Residue |
| A | HOH2032 |
| B | ASN484 |
| B | GLY532 |
| B | GOL1741 |
| A | GLY58 |
| A | PHE59 |
| site_id | CC8 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE GOL B 1745 |
| Chain | Residue |
| B | HIS320 |
| B | GLU321 |
| B | GLN572 |
| B | PHE638 |
| B | HOH2376 |
| site_id | CC9 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE GOL A 1746 |
| Chain | Residue |
| A | HIS203 |
| A | GLN676 |
| A | ARG718 |
| A | HOH2453 |
| A | HOH2454 |
| B | ASP56 |
| B | GLY58 |
| B | HOH2046 |
| site_id | DC1 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE GOL A 1747 |
| Chain | Residue |
| A | ARG325 |
| A | SER326 |
| A | VAL519 |
| A | THR520 |
| A | HOH2337 |
| A | HOH2455 |
| A | HOH2456 |
| site_id | DC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE GOL B 1746 |
| Chain | Residue |
| B | LYS457 |
| B | ARG460 |
| B | ASP461 |
| B | ASP513 |
| B | LEU514 |
| B | LYS517 |
Functional Information from PROSITE/UniProt
| site_id | PS00512 |
| Number of Residues | 16 |
| Details | ALPHA_GALACTOSIDASE Alpha-galactosidase signature. GLemFvLDDg.Wfgh....RD |
| Chain | Residue | Details |
| A | GLY363-ASP378 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | ACT_SITE: Nucleophile => ECO:0000305|PubMed:21827767 |
| Chain | Residue | Details |
| A | ASP482 | |
| B | ASP482 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | ACT_SITE: Proton donor => ECO:0000305|PubMed:21827767 |
| Chain | Residue | Details |
| A | ASP552 | |
| B | ASP552 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 12 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:21827767, ECO:0007744|PDB:2XN2 |
| Chain | Residue | Details |
| A | ASP370 | |
| B | LYS480 | |
| B | CYS530 | |
| B | ASP552 | |
| A | TRP415 | |
| A | ARG447 | |
| A | LYS480 | |
| A | CYS530 | |
| A | ASP552 | |
| B | ASP370 | |
| B | TRP415 | |
| B | ARG447 |
