4MAF
Soybean ATP Sulfurylase
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0000103 | biological_process | sulfate assimilation |
A | 0004781 | molecular_function | sulfate adenylyltransferase (ATP) activity |
B | 0000103 | biological_process | sulfate assimilation |
B | 0004781 | molecular_function | sulfate adenylyltransferase (ATP) activity |
C | 0000103 | biological_process | sulfate assimilation |
C | 0004781 | molecular_function | sulfate adenylyltransferase (ATP) activity |
D | 0000103 | biological_process | sulfate assimilation |
D | 0004781 | molecular_function | sulfate adenylyltransferase (ATP) activity |
E | 0000103 | biological_process | sulfate assimilation |
E | 0004781 | molecular_function | sulfate adenylyltransferase (ATP) activity |
F | 0000103 | biological_process | sulfate assimilation |
F | 0004781 | molecular_function | sulfate adenylyltransferase (ATP) activity |
G | 0000103 | biological_process | sulfate assimilation |
G | 0004781 | molecular_function | sulfate adenylyltransferase (ATP) activity |
H | 0000103 | biological_process | sulfate assimilation |
H | 0004781 | molecular_function | sulfate adenylyltransferase (ATP) activity |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 17 |
Details | BINDING SITE FOR RESIDUE ADX A 900 |
Chain | Residue |
A | PHE245 |
A | GLY348 |
A | ARG349 |
A | PRO351 |
A | ALA352 |
A | ARG388 |
A | VAL389 |
A | ALA390 |
A | HOH1027 |
A | GLN246 |
A | LEU247 |
A | ARG248 |
A | ASN249 |
A | HIS255 |
A | LEU258 |
A | MET322 |
A | VAL347 |
site_id | AC2 |
Number of Residues | 19 |
Details | BINDING SITE FOR RESIDUE ADX B 900 |
Chain | Residue |
B | PHE245 |
B | GLN246 |
B | LEU247 |
B | ARG248 |
B | ASN249 |
B | HIS255 |
B | LEU258 |
B | MET322 |
B | VAL347 |
B | GLY348 |
B | ARG349 |
B | PRO351 |
B | ALA352 |
B | ARG388 |
B | VAL389 |
B | ALA390 |
B | HOH1004 |
B | HOH1008 |
B | HOH1109 |
site_id | AC3 |
Number of Residues | 19 |
Details | BINDING SITE FOR RESIDUE ADX C 900 |
Chain | Residue |
C | PHE245 |
C | GLN246 |
C | LEU247 |
C | ARG248 |
C | ASN249 |
C | HIS255 |
C | LEU258 |
C | MET322 |
C | GLY348 |
C | ARG349 |
C | PRO351 |
C | ALA352 |
C | ARG388 |
C | VAL389 |
C | ALA390 |
C | HOH1014 |
C | HOH1021 |
C | HOH1064 |
C | HOH1134 |
site_id | AC4 |
Number of Residues | 20 |
Details | BINDING SITE FOR RESIDUE ADX D 900 |
Chain | Residue |
D | PHE245 |
D | GLN246 |
D | LEU247 |
D | ARG248 |
D | ASN249 |
D | HIS255 |
D | LEU258 |
D | MET322 |
D | VAL347 |
D | GLY348 |
D | ARG349 |
D | PRO351 |
D | ALA352 |
D | ARG388 |
D | VAL389 |
D | ALA390 |
D | HOH1019 |
D | HOH1032 |
D | HOH1066 |
D | HOH1084 |
site_id | AC5 |
Number of Residues | 17 |
Details | BINDING SITE FOR RESIDUE ADX E 900 |
Chain | Residue |
E | PHE245 |
E | GLN246 |
E | LEU247 |
E | ARG248 |
E | ASN249 |
E | HIS255 |
E | LEU258 |
E | MET322 |
E | GLY348 |
E | ARG349 |
E | PRO351 |
E | ALA352 |
E | ARG388 |
E | VAL389 |
E | ALA390 |
E | HOH1095 |
E | HOH1106 |
site_id | AC6 |
Number of Residues | 16 |
Details | BINDING SITE FOR RESIDUE ADX F 900 |
Chain | Residue |
F | MET322 |
F | GLY348 |
F | ARG349 |
F | PRO351 |
F | ALA352 |
F | ARG388 |
F | VAL389 |
F | ALA390 |
F | HOH1036 |
F | PHE245 |
F | GLN246 |
F | LEU247 |
F | ARG248 |
F | ASN249 |
F | HIS255 |
F | LEU258 |
site_id | AC7 |
Number of Residues | 16 |
Details | BINDING SITE FOR RESIDUE ADX G 900 |
Chain | Residue |
G | PHE245 |
G | GLN246 |
G | LEU247 |
G | ARG248 |
G | ASN249 |
G | HIS255 |
G | LEU258 |
G | MET322 |
G | GLY348 |
G | ARG349 |
G | PRO351 |
G | ALA352 |
G | ARG388 |
G | VAL389 |
G | ALA390 |
G | HOH1018 |
site_id | AC8 |
Number of Residues | 16 |
Details | BINDING SITE FOR RESIDUE ADX H 900 |
Chain | Residue |
H | PHE245 |
H | GLN246 |
H | LEU247 |
H | ARG248 |
H | ASN249 |
H | HIS255 |
H | LEU258 |
H | MET322 |
H | VAL347 |
H | GLY348 |
H | ARG349 |
H | PRO351 |
H | ALA352 |
H | ARG388 |
H | VAL389 |
H | ALA390 |