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 | 0004781 | molecular_function | sulfate adenylyltransferase (ATP) activity |
A | 0005524 | molecular_function | ATP binding |
A | 0005737 | cellular_component | cytoplasm |
A | 0005739 | cellular_component | mitochondrion |
A | 0006790 | biological_process | sulfur compound metabolic process |
A | 0010134 | biological_process | sulfate assimilation via adenylyl sulfate reduction |
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 | 0004781 | molecular_function | sulfate adenylyltransferase (ATP) activity |
B | 0005524 | molecular_function | ATP binding |
B | 0005737 | cellular_component | cytoplasm |
B | 0005739 | cellular_component | mitochondrion |
B | 0006790 | biological_process | sulfur compound metabolic process |
B | 0010134 | biological_process | sulfate assimilation via adenylyl sulfate reduction |
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 |