1FWK
CRYSTAL STRUCTURE OF HOMOSERINE KINASE COMPLEXED WITH ADP
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0000166 | molecular_function | nucleotide binding |
A | 0004413 | molecular_function | homoserine kinase activity |
A | 0005524 | molecular_function | ATP binding |
A | 0005737 | cellular_component | cytoplasm |
A | 0006566 | biological_process | threonine metabolic process |
A | 0008652 | biological_process | amino acid biosynthetic process |
A | 0009088 | biological_process | threonine biosynthetic process |
A | 0016301 | molecular_function | kinase activity |
A | 0016740 | molecular_function | transferase activity |
B | 0000166 | molecular_function | nucleotide binding |
B | 0004413 | molecular_function | homoserine kinase activity |
B | 0005524 | molecular_function | ATP binding |
B | 0005737 | cellular_component | cytoplasm |
B | 0006566 | biological_process | threonine metabolic process |
B | 0008652 | biological_process | amino acid biosynthetic process |
B | 0009088 | biological_process | threonine biosynthetic process |
B | 0016301 | molecular_function | kinase activity |
B | 0016740 | molecular_function | transferase activity |
C | 0000166 | molecular_function | nucleotide binding |
C | 0004413 | molecular_function | homoserine kinase activity |
C | 0005524 | molecular_function | ATP binding |
C | 0005737 | cellular_component | cytoplasm |
C | 0006566 | biological_process | threonine metabolic process |
C | 0008652 | biological_process | amino acid biosynthetic process |
C | 0009088 | biological_process | threonine biosynthetic process |
C | 0016301 | molecular_function | kinase activity |
C | 0016740 | molecular_function | transferase activity |
D | 0000166 | molecular_function | nucleotide binding |
D | 0004413 | molecular_function | homoserine kinase activity |
D | 0005524 | molecular_function | ATP binding |
D | 0005737 | cellular_component | cytoplasm |
D | 0006566 | biological_process | threonine metabolic process |
D | 0008652 | biological_process | amino acid biosynthetic process |
D | 0009088 | biological_process | threonine biosynthetic process |
D | 0016301 | molecular_function | kinase activity |
D | 0016740 | molecular_function | transferase activity |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE MG D 597 |
Chain | Residue |
D | SER98 |
D | SER134 |
D | ADP900 |
D | HOH996 |
D | HOH1007 |
site_id | AC2 |
Number of Residues | 19 |
Details | BINDING SITE FOR RESIDUE ADP A 600 |
Chain | Residue |
A | LYS87 |
A | ALA91 |
A | GLY92 |
A | GLY96 |
A | SER97 |
A | SER98 |
A | SER101 |
A | SER133 |
A | THR183 |
A | HOH604 |
A | HOH615 |
A | HOH616 |
A | HOH630 |
A | HOH642 |
A | HOH726 |
A | PRO56 |
A | LYS61 |
A | ASN62 |
A | VAL63 |
site_id | AC3 |
Number of Residues | 14 |
Details | BINDING SITE FOR RESIDUE ADP B 700 |
Chain | Residue |
B | PRO56 |
B | ASN62 |
B | VAL63 |
B | ALA91 |
B | GLY92 |
B | SER97 |
B | SER98 |
B | SER101 |
B | THR183 |
B | HOH709 |
B | HOH717 |
B | HOH728 |
B | HOH729 |
B | HOH801 |
site_id | AC4 |
Number of Residues | 18 |
Details | BINDING SITE FOR RESIDUE ADP C 800 |
Chain | Residue |
C | ILE55 |
C | LYS61 |
C | ASN62 |
C | VAL63 |
C | LYS87 |
C | ALA91 |
C | GLY92 |
C | SER97 |
C | SER98 |
C | SER101 |
C | SER133 |
C | HOH806 |
C | HOH830 |
C | HOH834 |
C | HOH852 |
C | HOH905 |
C | HOH951 |
C | HOH967 |
site_id | AC5 |
Number of Residues | 19 |
Details | BINDING SITE FOR RESIDUE ADP D 900 |
Chain | Residue |
D | ASN54 |
D | ILE55 |
D | PRO56 |
D | LYS61 |
D | ASN62 |
D | VAL63 |
D | LYS87 |
D | ALA91 |
D | GLY92 |
D | SER97 |
D | SER98 |
D | SER101 |
D | SER133 |
D | THR183 |
D | MG597 |
D | HOH903 |
D | HOH914 |
D | HOH927 |
D | HOH1042 |
Functional Information from PROSITE/UniProt
site_id | PS00627 |
Number of Residues | 12 |
Details | GHMP_KINASES_ATP GHMP kinases putative ATP-binding domain. VKaGsGLGSSAA |
Chain | Residue | Details |
A | VAL89-ALA100 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 40 |
Details | Binding site: {"evidences":[{"evidenceCode":"ECO:0000255"}]} |
Chain | Residue | Details |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 1 |
Details | a catalytic site defined by CSA, PubMed 11535056 |
Chain | Residue | Details |
D | THR183 |
site_id | CSA2 |
Number of Residues | 1 |
Details | a catalytic site defined by CSA, PubMed 11535056 |
Chain | Residue | Details |
A | THR183 |
site_id | CSA3 |
Number of Residues | 1 |
Details | a catalytic site defined by CSA, PubMed 11535056 |
Chain | Residue | Details |
B | THR183 |
site_id | CSA4 |
Number of Residues | 1 |
Details | a catalytic site defined by CSA, PubMed 11535056 |
Chain | Residue | Details |
C | THR183 |
site_id | MCSA1 |
Number of Residues | 2 |
Details | M-CSA 778 |
Chain | Residue | Details |
A | GLU130 | metal ligand |
A | THR183 | electrostatic stabiliser, polar interaction |
site_id | MCSA2 |
Number of Residues | 2 |
Details | M-CSA 778 |
Chain | Residue | Details |
B | GLU130 | metal ligand |
B | THR183 | electrostatic stabiliser, polar interaction |
site_id | MCSA3 |
Number of Residues | 2 |
Details | M-CSA 778 |
Chain | Residue | Details |
C | GLU130 | metal ligand |
C | THR183 | electrostatic stabiliser, polar interaction |
site_id | MCSA4 |
Number of Residues | 2 |
Details | M-CSA 778 |
Chain | Residue | Details |
D | GLU130 | metal ligand |
D | THR183 | electrostatic stabiliser, polar interaction |