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 |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE CD A 512 |
Chain | Residue |
A | ASP168 |
A | HIS235 |
A | HIS236 |
A | SO4525 |
A | ACY535 |
site_id | AC2 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE CD A 513 |
Chain | Residue |
A | HOH1094 |
A | HOH1102 |
A | PRO39 |
A | CYS43 |
A | HOH895 |
A | HOH1021 |
site_id | AC3 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE CD A 514 |
Chain | Residue |
A | LEU18 |
A | GLU22 |
A | HIS319 |
A | ACY526 |
A | HOH1033 |
site_id | AC4 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE CD A 515 |
Chain | Residue |
A | GLU182 |
A | GLU182 |
A | ACY533 |
A | ACY533 |
site_id | AC5 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE CD A 516 |
Chain | Residue |
A | ASP189 |
A | HIS494 |
A | ACY527 |
A | ACY534 |
site_id | AC6 |
Number of Residues | 1 |
Details | BINDING SITE FOR RESIDUE CA A 517 |
site_id | AC7 |
Number of Residues | 1 |
Details | BINDING SITE FOR RESIDUE NA A 518 |
site_id | AC8 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE CA A 519 |
Chain | Residue |
A | ASP303 |
A | ACY536 |
site_id | AC9 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE CA A 520 |
Chain | Residue |
A | ASP489 |
A | ASP489 |
site_id | BC1 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE MG A 521 |
Chain | Residue |
A | GLU46 |
A | PRO164 |
A | HIS166 |
A | HOH604 |
A | HOH1101 |
site_id | BC2 |
Number of Residues | 1 |
Details | BINDING SITE FOR RESIDUE NA A 522 |
site_id | BC3 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE SO4 A 523 |
Chain | Residue |
A | GLN195 |
A | ARG197 |
A | ALA293 |
A | HOH779 |
A | HOH809 |
A | HOH990 |
site_id | BC4 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE SO4 A 525 |
Chain | Residue |
A | HIS166 |
A | ASP168 |
A | ARG173 |
A | HIS235 |
A | SER417 |
A | CD512 |
A | ACY535 |
A | HOH553 |
A | HOH733 |
site_id | BC5 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE TRS A 524 |
Chain | Residue |
A | PRO2 |
A | ASP189 |
A | GLY282 |
A | HOH617 |
A | HOH874 |
site_id | BC6 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE ACY A 526 |
Chain | Residue |
A | ALA17 |
A | LEU18 |
A | LYS20 |
A | ASN21 |
A | GLU22 |
A | HIS319 |
A | CD514 |
A | HOH812 |
site_id | BC7 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE ACY A 527 |
Chain | Residue |
A | GLN187 |
A | ASP189 |
A | SER493 |
A | HIS494 |
A | CD516 |
A | ACY534 |
A | HOH692 |
site_id | BC8 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE ACY A 528 |
Chain | Residue |
A | ASN216 |
A | GLU486 |
A | GLU490 |
A | PRO491 |
A | HIS494 |
A | LYS498 |
site_id | BC9 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE ACY A 529 |
Chain | Residue |
A | LYS174 |
A | GLN178 |
A | LEU181 |
A | GLU182 |
A | GLU182 |
A | SER185 |
site_id | CC1 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE ACY A 530 |
Chain | Residue |
A | GLU130 |
A | ARG134 |
site_id | CC2 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE ACY A 531 |
Chain | Residue |
A | PRO55 |
A | LEU56 |
A | THR57 |
A | GLY58 |
A | ASP64 |
A | HOH719 |
site_id | CC3 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE ACY A 532 |
site_id | CC4 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE ACY A 533 |
Chain | Residue |
A | CD515 |
A | CD515 |
A | HOH561 |
A | GLY171 |
A | LYS174 |
A | GLU182 |
A | GLU182 |
A | ARG186 |
A | PHE255 |
site_id | CC5 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE ACY A 534 |
Chain | Residue |
A | ASP189 |
A | HIS494 |
A | CD516 |
A | ACY527 |
A | HOH671 |
site_id | CC6 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE ACY A 535 |
Chain | Residue |
A | ASP168 |
A | HIS235 |
A | HIS236 |
A | SER417 |
A | CD512 |
A | SO4525 |
site_id | CC7 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE ACY A 536 |
Chain | Residue |
A | LYS297 |
A | GLY301 |
A | VAL302 |
A | ASP303 |
A | CA519 |
Functional Information from SwissProt/UniProt
Chain | Residue | Details |
A | THR196 | |
A | ARG197 | |
A | ASN198 | |
Chain | Residue | Details |
A | GLN195 | |
A | ARG197 | |
A | GLY289 | |
A | ALA293 | |
A | VAL331 | |
Chain | Residue | Details |
A | HIS201 | |
A | HIS204 | |
Chain | Residue | Details |
A | PHE328 | |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 1 |
Details | a catalytic site defined by CSA, PubMed 11157739 |
Chain | Residue | Details |
A | 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 |