1JED
Crystal Structure of ATP Sulfurylase in complex with ADP
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000096 | biological_process | sulfur amino acid metabolic process |
| A | 0000103 | biological_process | sulfate assimilation |
| A | 0000166 | molecular_function | nucleotide binding |
| A | 0004781 | molecular_function | sulfate adenylyltransferase (ATP) activity |
| A | 0005524 | molecular_function | ATP binding |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005739 | cellular_component | mitochondrion |
| A | 0016740 | molecular_function | transferase activity |
| A | 0016779 | molecular_function | nucleotidyltransferase activity |
| A | 0019379 | biological_process | sulfate assimilation, phosphoadenylyl sulfate reduction by phosphoadenylyl-sulfate reductase (thioredoxin) |
| A | 0070814 | biological_process | hydrogen sulfide biosynthetic process |
| B | 0000096 | biological_process | sulfur amino acid metabolic process |
| B | 0000103 | biological_process | sulfate assimilation |
| B | 0000166 | molecular_function | nucleotide binding |
| B | 0004781 | molecular_function | sulfate adenylyltransferase (ATP) activity |
| B | 0005524 | molecular_function | ATP binding |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0005739 | cellular_component | mitochondrion |
| B | 0016740 | molecular_function | transferase activity |
| B | 0016779 | molecular_function | nucleotidyltransferase activity |
| B | 0019379 | biological_process | sulfate assimilation, phosphoadenylyl sulfate reduction by phosphoadenylyl-sulfate reductase (thioredoxin) |
| B | 0070814 | biological_process | hydrogen sulfide biosynthetic process |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CD A 512 |
| Chain | Residue |
| A | ASP168 |
| A | HIS235 |
| A | HIS236 |
| A | ACY557 |
| site_id | AC2 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE CD A 513 |
| Chain | Residue |
| A | PRO39 |
| A | CYS43 |
| A | HOH1213 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CD A 514 |
| Chain | Residue |
| A | ACY551 |
| A | HOH673 |
| B | HIS319 |
| A | LEU18 |
| A | GLU22 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CD A 515 |
| Chain | Residue |
| A | GLU182 |
| A | ACY555 |
| B | GLU182 |
| B | CD533 |
| B | ACY562 |
| site_id | AC5 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CD A 516 |
| Chain | Residue |
| A | ASP189 |
| A | HIS494 |
| A | ACY552 |
| A | ACY556 |
| site_id | AC6 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE CA A 517 |
| Chain | Residue |
| A | ASP151 |
| A | HOH905 |
| site_id | AC7 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE NA A 518 |
| Chain | Residue |
| A | HOH947 |
| A | HOH1083 |
| B | GLU409 |
| site_id | AC8 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE CA A 519 |
| Chain | Residue |
| A | LYS297 |
| A | ASP303 |
| site_id | AC9 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE CA A 520 |
| Chain | Residue |
| A | ASP489 |
| A | ASP489 |
| A | HOH753 |
| site_id | BC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE MG A 521 |
| Chain | Residue |
| A | GLU46 |
| A | PRO164 |
| A | HIS166 |
| A | HOH1123 |
| site_id | BC2 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE NA A 522 |
| Chain | Residue |
| A | ASP309 |
| A | HOH1174 |
| site_id | BC3 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE NA A 523 |
| Chain | Residue |
| A | ASP322 |
| A | HOH1139 |
| site_id | BC4 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CD A 524 |
| Chain | Residue |
| A | ASP71 |
| A | ACY565 |
| A | HOH681 |
| A | HOH732 |
| B | THR70 |
| B | ASP71 |
| site_id | BC5 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE NA A 525 |
| Chain | Residue |
| A | GLU130 |
| A | HOH654 |
| A | HOH1022 |
| B | ASN124 |
| site_id | BC6 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE NA A 526 |
| Chain | Residue |
| A | GLU324 |
| site_id | BC7 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE NA A 527 |
| Chain | Residue |
| A | ASP505 |
| A | HOH1036 |
| A | HOH1104 |
| site_id | BC8 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE MG A 539 |
| Chain | Residue |
| A | ADP635 |
| site_id | BC9 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CD B 530 |
| Chain | Residue |
| B | ASP168 |
| B | HIS235 |
| B | HIS236 |
| B | ACY564 |
| site_id | CC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CD B 531 |
| Chain | Residue |
| B | PRO39 |
| B | CYS43 |
| B | HOH1117 |
| B | HOH1142 |
| site_id | CC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CD B 532 |
| Chain | Residue |
| A | HIS319 |
| B | LEU18 |
| B | GLU22 |
| B | ACY558 |
| site_id | CC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CD B 533 |
| Chain | Residue |
| A | LYS174 |
| A | GLU182 |
| A | CD515 |
| A | ACY555 |
| B | GLU182 |
| B | ACY562 |
| site_id | CC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CD B 534 |
| Chain | Residue |
| B | ASP189 |
| B | HIS494 |
| B | ACY559 |
| B | ACY563 |
| site_id | CC5 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE CA B 535 |
| Chain | Residue |
| B | ASP151 |
| B | HOH908 |
| B | HOH1027 |
| site_id | CC6 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE NA B 540 |
| Chain | Residue |
| A | GLU409 |
| B | HOH853 |
| site_id | CC7 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE CA B 537 |
| Chain | Residue |
| B | LYS297 |
| B | ASP303 |
| site_id | CC8 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE CA B 538 |
| Chain | Residue |
| B | ASP489 |
| B | ASP489 |
| site_id | CC9 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE MG B 547 |
| Chain | Residue |
| B | GLU46 |
| B | PRO164 |
| B | GLN165 |
| B | HIS166 |
| site_id | DC1 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE NA B 541 |
| Chain | Residue |
| B | ASP309 |
| B | HOH1031 |
| site_id | DC2 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE NA B 542 |
| Chain | Residue |
| B | GLU324 |
| B | HOH823 |
| site_id | DC3 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE NA B 543 |
| Chain | Residue |
| B | ASP322 |
| B | HOH1002 |
| site_id | DC4 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE NA B 544 |
| Chain | Residue |
| B | ASP322 |
| B | HOH939 |
| site_id | DC5 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE NA B 545 |
| Chain | Residue |
| B | ASP505 |
| B | HOH1156 |
| site_id | DC6 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE MG B 546 |
| Chain | Residue |
| B | ARG197 |
| B | ADP636 |
| site_id | DC7 |
| Number of Residues | 16 |
| Details | BINDING SITE FOR RESIDUE ADP A 635 |
| Chain | Residue |
| A | PHE194 |
| A | GLN195 |
| A | THR196 |
| A | ARG197 |
| A | ASN198 |
| A | HIS204 |
| A | LEU207 |
| A | GLY289 |
| A | ARG290 |
| A | HIS292 |
| A | ALA293 |
| A | ARG329 |
| A | MET330 |
| A | VAL331 |
| A | MG539 |
| A | HOH1212 |
| site_id | DC8 |
| Number of Residues | 17 |
| Details | BINDING SITE FOR RESIDUE ADP B 636 |
| Chain | Residue |
| B | PHE194 |
| B | GLN195 |
| B | THR196 |
| B | ARG197 |
| B | ASN198 |
| B | HIS204 |
| B | LEU207 |
| B | GLY289 |
| B | ARG290 |
| B | HIS292 |
| B | ALA293 |
| B | ARG329 |
| B | MET330 |
| B | VAL331 |
| B | MG546 |
| B | HOH783 |
| B | HOH1053 |
| site_id | DC9 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE TRS A 1415 |
| Chain | Residue |
| A | VAL225 |
| A | GLY226 |
| A | THR228 |
| A | ASP232 |
| A | ILE233 |
| A | ASP234 |
| A | HIS235 |
| A | ARG238 |
| A | HOH738 |
| site_id | EC1 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE TRS B 1416 |
| Chain | Residue |
| B | VAL225 |
| B | GLY226 |
| B | THR228 |
| B | ASP232 |
| B | ILE233 |
| B | HIS235 |
| B | ARG238 |
| site_id | EC2 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE ACY A 551 |
| Chain | Residue |
| A | ALA17 |
| A | LEU18 |
| A | LYS19 |
| A | LYS20 |
| A | ASN21 |
| A | GLU22 |
| A | CD514 |
| B | HIS319 |
| site_id | EC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE ACY A 552 |
| Chain | Residue |
| A | ASP189 |
| A | SER493 |
| A | HIS494 |
| A | CD516 |
| A | ACY556 |
| site_id | EC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ACY A 553 |
| Chain | Residue |
| A | ASN216 |
| A | GLU486 |
| A | GLU490 |
| A | HIS494 |
| site_id | EC5 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE ACY A 554 |
| Chain | Residue |
| A | LYS174 |
| A | GLN178 |
| A | GLU182 |
| B | GLU182 |
| B | SER185 |
| B | ACY561 |
| site_id | EC6 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE ACY A 555 |
| Chain | Residue |
| A | ARG186 |
| A | CD515 |
| A | HOH1110 |
| B | LEU172 |
| B | LYS174 |
| B | PHE255 |
| B | CD533 |
| B | ACY562 |
| B | HOH897 |
| site_id | EC7 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE ACY A 556 |
| Chain | Residue |
| A | ASP189 |
| A | HIS494 |
| A | CD516 |
| A | ACY552 |
| A | HOH756 |
| site_id | EC8 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ACY A 557 |
| Chain | Residue |
| A | HIS236 |
| A | CD512 |
| B | SER417 |
| B | LEU420 |
| site_id | EC9 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE ACY B 558 |
| Chain | Residue |
| A | HIS319 |
| B | LEU18 |
| B | LYS20 |
| B | ASN21 |
| B | GLU22 |
| B | CD532 |
| site_id | FC1 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE ACY B 559 |
| Chain | Residue |
| B | GLN187 |
| B | ASP189 |
| B | PRO491 |
| B | SER493 |
| B | HIS494 |
| B | CD534 |
| B | ACY563 |
| site_id | FC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE ACY B 560 |
| Chain | Residue |
| B | ASN216 |
| B | GLU486 |
| B | GLU490 |
| B | HIS494 |
| B | HOH978 |
| site_id | FC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE ACY B 561 |
| Chain | Residue |
| A | GLU182 |
| A | SER185 |
| A | ACY554 |
| B | LYS174 |
| B | GLU182 |
| site_id | FC4 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE ACY B 562 |
| Chain | Residue |
| A | GLY171 |
| A | LEU172 |
| A | LYS174 |
| A | GLU182 |
| A | PHE255 |
| A | CD515 |
| A | ACY555 |
| B | GLU182 |
| B | ARG186 |
| B | CD533 |
| B | HOH701 |
| site_id | FC5 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE ACY B 563 |
| Chain | Residue |
| B | ASP189 |
| B | ARG190 |
| B | HIS494 |
| B | CD534 |
| B | ACY559 |
| B | HOH724 |
| B | HOH809 |
| site_id | FC6 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE ACY B 564 |
| Chain | Residue |
| A | SER417 |
| B | ASP168 |
| B | HIS236 |
| B | CD530 |
| B | HOH936 |
| site_id | FC7 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE ACY A 565 |
| Chain | Residue |
| A | ASP71 |
| A | ARG73 |
| A | CD524 |
| A | HOH732 |
| A | HOH881 |
| B | ASP71 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 6 |
| Details | ACT_SITE: ACT_SITE => ECO:0000255|HAMAP-Rule:MF_03106, ECO:0000305|PubMed:11157739 |
| Chain | Residue | Details |
| A | THR196 | |
| A | ARG197 | |
| A | ASN198 | |
| B | THR196 | |
| B | ARG197 | |
| B | ASN198 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 10 |
| Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_03106, ECO:0000269|PubMed:11157739 |
| Chain | Residue | Details |
| A | GLN195 | |
| B | VAL331 | |
| A | ARG197 | |
| A | GLY289 | |
| A | ALA293 | |
| A | VAL331 | |
| B | GLN195 | |
| B | ARG197 | |
| B | GLY289 | |
| B | ALA293 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 4 |
| Details | SITE: Transition state stabilizer => ECO:0000255|HAMAP-Rule:MF_03106, ECO:0000305|PubMed:11157739 |
| Chain | Residue | Details |
| A | HIS201 | |
| A | HIS204 | |
| B | HIS201 | |
| B | HIS204 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | SITE: Induces change in substrate recognition on ATP binding => ECO:0000255|HAMAP-Rule:MF_03106, ECO:0000305|PubMed:11157739 |
| Chain | Residue | Details |
| A | PHE328 | |
| B | PHE328 |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1j70 |
| Chain | Residue | Details |
| A | HIS204 | |
| A | HIS201 | |
| A | ARG197 |
| site_id | CSA2 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1j70 |
| Chain | Residue | Details |
| B | HIS204 | |
| B | HIS201 | |
| B | ARG197 |
| site_id | CSA3 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1j70 |
| Chain | Residue | Details |
| A | ARG290 |
| site_id | CSA4 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1j70 |
| Chain | Residue | Details |
| B | ARG290 |
| site_id | MCSA1 |
| Number of Residues | 5 |
| Details | M-CSA 287 |
| Chain | Residue | Details |
| A | THR196 | electrostatic stabiliser, hydrogen bond donor, steric role |
| A | ARG197 | electrostatic stabiliser, hydrogen bond donor, steric role |
| A | HIS201 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
| A | HIS204 | electrostatic stabiliser |
| A | ARG290 | electrostatic stabiliser |
| site_id | MCSA2 |
| Number of Residues | 5 |
| Details | M-CSA 287 |
| Chain | Residue | Details |
| B | THR196 | electrostatic stabiliser, hydrogen bond donor, steric role |
| B | ARG197 | electrostatic stabiliser, hydrogen bond donor, steric role |
| B | HIS201 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
| B | HIS204 | electrostatic stabiliser |
| B | ARG290 | electrostatic stabiliser |
