2XHN
Rhamnogalacturonan lyase from Aspergillus aculeatus K150A active site mutant
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0000272 | biological_process | polysaccharide catabolic process |
A | 0003824 | molecular_function | catalytic activity |
A | 0005576 | cellular_component | extracellular region |
A | 0005975 | biological_process | carbohydrate metabolic process |
A | 0016829 | molecular_function | lyase activity |
A | 0016837 | molecular_function | carbon-oxygen lyase activity, acting on polysaccharides |
A | 0030246 | molecular_function | carbohydrate binding |
A | 0045490 | biological_process | pectin catabolic process |
A | 0071555 | biological_process | cell wall organization |
A | 0102210 | molecular_function | rhamnogalacturonan endolyase activity |
B | 0000272 | biological_process | polysaccharide catabolic process |
B | 0003824 | molecular_function | catalytic activity |
B | 0005576 | cellular_component | extracellular region |
B | 0005975 | biological_process | carbohydrate metabolic process |
B | 0016829 | molecular_function | lyase activity |
B | 0016837 | molecular_function | carbon-oxygen lyase activity, acting on polysaccharides |
B | 0030246 | molecular_function | carbohydrate binding |
B | 0045490 | biological_process | pectin catabolic process |
B | 0071555 | biological_process | cell wall organization |
B | 0102210 | molecular_function | rhamnogalacturonan endolyase activity |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE CA A 800 |
Chain | Residue |
A | GLU347 |
A | ASP349 |
A | GLN351 |
A | ASP502 |
A | HOH2761 |
site_id | AC2 |
Number of Residues | 11 |
Details | BINDING SITE FOR RESIDUE SO4 A 901 |
Chain | Residue |
A | GLY232 |
A | HOH2067 |
A | HOH2571 |
A | HOH2941 |
A | HOH2942 |
A | HOH2943 |
A | HOH2945 |
A | ASN19 |
A | SER229 |
A | ARG230 |
A | SER231 |
site_id | AC3 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE SO4 A 902 |
Chain | Residue |
A | LYS395 |
A | LYS395 |
A | SER490 |
A | SER490 |
A | HOH2946 |
A | HOH2947 |
A | HOH2948 |
site_id | AC4 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE SO4 A 903 |
Chain | Residue |
A | ARG429 |
A | GLY488 |
A | HOH2949 |
A | HOH2951 |
A | HOH2952 |
site_id | AC5 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE SO4 A 904 |
Chain | Residue |
A | SER53 |
A | ARG107 |
A | ARG111 |
A | HOH2537 |
A | HOH2954 |
site_id | AC6 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE EDO A 1509 |
Chain | Residue |
A | SER369 |
A | SER369 |
A | HOH2775 |
A | HOH2777 |
A | HOH2955 |
A | HOH2955 |
A | HOH2956 |
site_id | AC7 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE CA B 801 |
Chain | Residue |
B | GLU347 |
B | ASP349 |
B | GLN351 |
B | ASP502 |
B | HOH2725 |
site_id | AC8 |
Number of Residues | 10 |
Details | BINDING SITE FOR RESIDUE SO4 B 905 |
Chain | Residue |
B | ASN19 |
B | SER229 |
B | ARG230 |
B | SER231 |
B | GLY232 |
B | HOH2059 |
B | HOH2528 |
B | HOH2534 |
B | HOH2920 |
B | HOH2922 |
site_id | AC9 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE SO4 B 906 |
Chain | Residue |
B | LYS395 |
B | LYS395 |
B | SER490 |
B | SER490 |
B | HOH2780 |
B | HOH2780 |
B | HOH2781 |
B | HOH2781 |
site_id | BC1 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE SO4 B 907 |
Chain | Residue |
B | ARG429 |
B | GLY488 |
B | HOH2923 |
site_id | BC2 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE SO4 B 908 |
Chain | Residue |
B | GLN47 |
B | SER53 |
B | ARG107 |
B | ARG111 |
B | HOH2496 |
B | HOH2926 |
B | HOH2927 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 2 |
Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255 |
Chain | Residue | Details |
A | ASN331 | |
B | ASN331 |