3K8K
Crystal structure of SusG
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0000272 | biological_process | polysaccharide catabolic process |
A | 0000287 | molecular_function | magnesium ion binding |
A | 0004556 | molecular_function | alpha-amylase activity |
A | 0005509 | molecular_function | calcium ion binding |
A | 0005975 | biological_process | carbohydrate metabolic process |
A | 0005983 | biological_process | starch catabolic process |
A | 0009279 | cellular_component | cell outer membrane |
A | 0009313 | biological_process | oligosaccharide catabolic process |
A | 0016798 | molecular_function | hydrolase activity, acting on glycosyl bonds |
A | 0019867 | cellular_component | outer membrane |
A | 0046872 | molecular_function | metal ion binding |
A | 2001070 | molecular_function | starch binding |
B | 0000272 | biological_process | polysaccharide catabolic process |
B | 0000287 | molecular_function | magnesium ion binding |
B | 0004556 | molecular_function | alpha-amylase activity |
B | 0005509 | molecular_function | calcium ion binding |
B | 0005975 | biological_process | carbohydrate metabolic process |
B | 0005983 | biological_process | starch catabolic process |
B | 0009279 | cellular_component | cell outer membrane |
B | 0009313 | biological_process | oligosaccharide catabolic process |
B | 0016798 | molecular_function | hydrolase activity, acting on glycosyl bonds |
B | 0019867 | cellular_component | outer membrane |
B | 0046872 | molecular_function | metal ion binding |
B | 2001070 | molecular_function | starch binding |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE MG A 700 |
Chain | Residue |
A | ASP73 |
A | ASP75 |
A | ASP77 |
A | TYR79 |
A | ASP81 |
A | HOH1013 |
site_id | AC2 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE CA A 710 |
Chain | Residue |
A | ILE393 |
A | HOH709 |
A | HOH837 |
A | HOH838 |
A | ASN153 |
A | ASP352 |
A | HIS392 |
site_id | AC3 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE EDO A 900 |
Chain | Residue |
A | CYS108 |
A | SER110 |
A | ASN123 |
A | GLN125 |
A | HOH786 |
A | HOH893 |
site_id | AC4 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE EDO A 901 |
Chain | Residue |
A | HIS112 |
A | ASP498 |
A | ASP545 |
A | ARG549 |
A | HOH839 |
A | HOH840 |
A | ACT961 |
site_id | AC5 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE EDO A 902 |
Chain | Residue |
A | LYS541 |
A | ASP545 |
site_id | AC6 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE EDO A 903 |
Chain | Residue |
A | PRO172 |
A | TYR173 |
A | TYR176 |
A | HOH913 |
site_id | AC7 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE EDO A 904 |
Chain | Residue |
A | TYR203 |
A | ALA205 |
A | TRP208 |
site_id | AC8 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE EDO A 908 |
Chain | Residue |
A | TYR111 |
A | GLU546 |
A | TYR562 |
A | THR563 |
site_id | AC9 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE EDO A 910 |
Chain | Residue |
A | GLY381 |
A | ASP383 |
A | HIS422 |
A | HOH702 |
site_id | BC1 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE EDO A 911 |
Chain | Residue |
A | ASP372 |
A | HOH1001 |
B | LYS321 |
site_id | BC2 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE PEG A 951 |
Chain | Residue |
A | ASP52 |
A | SER593 |
A | ARG596 |
A | LEU661 |
A | PHE662 |
A | HOH891 |
site_id | BC3 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE ACT A 961 |
Chain | Residue |
A | HIS154 |
A | ASP388 |
A | HOH816 |
A | EDO901 |
site_id | BC4 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE ACT A 962 |
Chain | Residue |
A | SER110 |
A | HIS112 |
A | THR347 |
A | TRP349 |
site_id | BC5 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE ACT A 972 |
Chain | Residue |
A | ARG457 |
A | TRP460 |
site_id | BC6 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE ACT A 973 |
Chain | Residue |
A | GLU658 |
A | VAL660 |
A | GLN669 |
site_id | BC7 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE MG B 800 |
Chain | Residue |
B | ASP73 |
B | ASP75 |
B | ASP77 |
B | TYR79 |
B | ASP81 |
B | HOH805 |
site_id | BC8 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE CA B 810 |
Chain | Residue |
B | ASN153 |
B | ASP352 |
B | HIS392 |
B | ILE393 |
B | HOH746 |
B | HOH748 |
B | HOH749 |
site_id | BC9 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE EDO B 905 |
Chain | Residue |
B | CYS108 |
B | SER110 |
B | ASN123 |
B | GLN125 |
site_id | CC1 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE EDO B 906 |
Chain | Residue |
B | ASP545 |
B | ARG549 |
B | HOH779 |
site_id | CC2 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE EDO B 907 |
Chain | Residue |
B | TYR173 |
B | TYR176 |
B | PRO365 |
site_id | CC3 |
Number of Residues | 1 |
Details | BINDING SITE FOR RESIDUE EDO B 912 |
Chain | Residue |
B | ASN589 |
site_id | CC4 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE ACT B 971 |
Chain | Residue |
B | HIS154 |
B | PHE345 |
B | ASP388 |
B | HOH750 |
B | HOH779 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 2 |
Details | ACT_SITE: Nucleophile => ECO:0000250 |
Chain | Residue | Details |
A | ASP388 | |
B | ASP388 |
site_id | SWS_FT_FI2 |
Number of Residues | 2 |
Details | ACT_SITE: Proton donor => ECO:0000250 |
Chain | Residue | Details |
A | GLU431 | |
B | GLU431 |
site_id | SWS_FT_FI3 |
Number of Residues | 16 |
Details | BINDING: BINDING => ECO:0000269|PubMed:20159465 |
Chain | Residue | Details |
A | ASP73 | |
B | ASP75 | |
B | ASP77 | |
B | TYR79 | |
B | ASP81 | |
B | ASN153 | |
B | ASP352 | |
B | HIS392 | |
A | ASP75 | |
A | ASP77 | |
A | TYR79 | |
A | ASP81 | |
A | ASN153 | |
A | ASP352 | |
A | HIS392 | |
B | ASP73 |
site_id | SWS_FT_FI4 |
Number of Residues | 8 |
Details | SITE: Starch => ECO:0000305|PubMed:20159465 |
Chain | Residue | Details |
A | LYS304 | |
A | LYS472 | |
A | ASP545 | |
A | ARG549 | |
B | LYS304 | |
B | LYS472 | |
B | ASP545 | |
B | ARG549 |
site_id | SWS_FT_FI5 |
Number of Residues | 2 |
Details | SITE: Transition state stabilizer => ECO:0000305|PubMed:20159465 |
Chain | Residue | Details |
A | ASP498 | |
B | ASP498 |