5CB8
Crystal structure of Adenosine-5'-phosphosulfate kinase in complex with APS and sulfate
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000103 | biological_process | sulfate assimilation |
| A | 0004020 | molecular_function | adenylylsulfate kinase activity |
| A | 0004781 | molecular_function | sulfate adenylyltransferase (ATP) activity |
| A | 0005524 | molecular_function | ATP binding |
| A | 0010134 | biological_process | sulfate assimilation via adenylyl sulfate reduction |
| A | 0016301 | molecular_function | kinase activity |
| A | 0019379 | biological_process | sulfate assimilation, phosphoadenylyl sulfate reduction by phosphoadenylyl-sulfate reductase (thioredoxin) |
| A | 0070814 | biological_process | hydrogen sulfide biosynthetic process |
| B | 0000103 | biological_process | sulfate assimilation |
| B | 0004020 | molecular_function | adenylylsulfate kinase activity |
| B | 0004781 | molecular_function | sulfate adenylyltransferase (ATP) activity |
| B | 0005524 | molecular_function | ATP binding |
| B | 0010134 | biological_process | sulfate assimilation via adenylyl sulfate reduction |
| B | 0016301 | molecular_function | kinase 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 | 19 |
| Details | binding site for residue ADX A 301 |
| Chain | Residue |
| A | ASP42 |
| A | PRO87 |
| A | LYS120 |
| A | LEU122 |
| A | GLY133 |
| A | PHE134 |
| A | THR135 |
| A | HOH417 |
| A | HOH429 |
| A | HOH498 |
| A | HOH553 |
| A | ARG45 |
| A | PHE54 |
| A | ARG59 |
| A | ASN62 |
| A | ILE63 |
| A | ALA84 |
| A | ILE85 |
| A | SER86 |
| site_id | AC2 |
| Number of Residues | 10 |
| Details | binding site for residue SO4 A 302 |
| Chain | Residue |
| A | LEU13 |
| A | GLY15 |
| A | ALA16 |
| A | GLY17 |
| A | LYS18 |
| A | THR19 |
| A | HOH420 |
| A | HOH421 |
| A | HOH429 |
| A | HOH472 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | binding site for residue SO4 A 303 |
| Chain | Residue |
| A | THR61 |
| A | ARG64 |
| A | HOH448 |
| A | HOH456 |
| A | HOH475 |
| A | HOH536 |
| site_id | AC4 |
| Number of Residues | 3 |
| Details | binding site for residue ACT A 304 |
| Chain | Residue |
| A | HIS71 |
| A | ARG75 |
| A | HOH466 |
| site_id | AC5 |
| Number of Residues | 20 |
| Details | binding site for residue ADX B 301 |
| Chain | Residue |
| B | ASP42 |
| B | ARG45 |
| B | PHE54 |
| B | ARG59 |
| B | ASN62 |
| B | ILE63 |
| B | ALA84 |
| B | ILE85 |
| B | SER86 |
| B | PRO87 |
| B | LYS120 |
| B | LEU122 |
| B | GLY133 |
| B | PHE134 |
| B | THR135 |
| B | HOH413 |
| B | HOH418 |
| B | HOH489 |
| B | HOH496 |
| B | HOH525 |
| site_id | AC6 |
| Number of Residues | 11 |
| Details | binding site for residue SO4 B 302 |
| Chain | Residue |
| B | LEU13 |
| B | SER14 |
| B | GLY15 |
| B | ALA16 |
| B | GLY17 |
| B | LYS18 |
| B | THR19 |
| B | HOH407 |
| B | HOH413 |
| B | HOH424 |
| B | HOH449 |
| site_id | AC7 |
| Number of Residues | 9 |
| Details | binding site for residue SO4 B 303 |
| Chain | Residue |
| A | LYS50 |
| A | HOH452 |
| B | THR61 |
| B | ARG64 |
| B | HOH430 |
| B | HOH447 |
| B | HOH451 |
| B | HOH512 |
| B | HOH546 |
| site_id | AC8 |
| Number of Residues | 3 |
| Details | binding site for residue ACT B 304 |
| Chain | Residue |
| B | HIS71 |
| B | ARG75 |
| B | HOH501 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | ACT_SITE: Phosphoserine intermediate => ECO:0000250 |
| Chain | Residue | Details |
| A | SER86 | |
| B | SER86 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | BINDING: BINDING => ECO:0000250 |
| Chain | Residue | Details |
| A | GLY12 | |
| B | GLY12 |
