1H74
CRYSTAL STRUCTURE OF HOMOSERINE KINASE COMPLEXED WITH ILE
Functional Information from GO Data
Chain | GOid | namespace | contents |
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 | 0009088 | biological_process | threonine biosynthetic process |
A | 0016301 | molecular_function | kinase activity |
A | 0016310 | biological_process | phosphorylation |
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 | 0009088 | biological_process | threonine biosynthetic process |
B | 0016301 | molecular_function | kinase activity |
B | 0016310 | biological_process | phosphorylation |
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 | 0009088 | biological_process | threonine biosynthetic process |
C | 0016301 | molecular_function | kinase activity |
C | 0016310 | biological_process | phosphorylation |
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 | 0009088 | biological_process | threonine biosynthetic process |
D | 0016301 | molecular_function | kinase activity |
D | 0016310 | biological_process | phosphorylation |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE MG B 600 |
Chain | Residue |
B | SER98 |
B | GLU130 |
B | AGS400 |
site_id | AC2 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE ILE A 500 |
Chain | Residue |
A | THR183 |
A | ARG187 |
A | ARG235 |
A | ASN17 |
A | PHE22 |
A | ASP23 |
A | HIS138 |
A | ASP140 |
A | ASN141 |
site_id | AC3 |
Number of Residues | 12 |
Details | BINDING SITE FOR RESIDUE ILE B 500 |
Chain | Residue |
B | ALA16 |
B | ASN17 |
B | ASP23 |
B | HIS138 |
B | ASP140 |
B | ASN141 |
B | ARG187 |
B | ARG235 |
B | SER261 |
B | AGS400 |
B | HOH2007 |
B | HOH2060 |
site_id | AC4 |
Number of Residues | 10 |
Details | BINDING SITE FOR RESIDUE ILE C 500 |
Chain | Residue |
C | ALA16 |
C | ASN17 |
C | ASP23 |
C | HIS138 |
C | ASP140 |
C | ASN141 |
C | ARG187 |
C | ARG235 |
C | HOH2013 |
C | HOH2138 |
site_id | AC5 |
Number of Residues | 11 |
Details | BINDING SITE FOR RESIDUE ILE D 500 |
Chain | Residue |
D | ASN17 |
D | PHE22 |
D | ASP23 |
D | ASP140 |
D | THR183 |
D | ARG187 |
D | ARG235 |
D | AGS400 |
D | HOH2040 |
D | HOH2057 |
D | HOH2106 |
site_id | AC6 |
Number of Residues | 17 |
Details | BINDING SITE FOR RESIDUE ADP A 400 |
Chain | Residue |
A | ILE55 |
A | PRO56 |
A | LYS61 |
A | ASN62 |
A | VAL63 |
A | LYS87 |
A | ALA91 |
A | GLY92 |
A | SER97 |
A | SER98 |
A | SER101 |
A | SER133 |
A | THR183 |
A | HOH2102 |
A | HOH2103 |
A | HOH2104 |
A | HOH2105 |
site_id | AC7 |
Number of Residues | 19 |
Details | BINDING SITE FOR RESIDUE AGS B 400 |
Chain | Residue |
B | PRO56 |
B | ASN62 |
B | VAL63 |
B | LYS87 |
B | ALA91 |
B | GLY92 |
B | GLY94 |
B | GLY96 |
B | SER97 |
B | SER98 |
B | SER101 |
B | SER133 |
B | ASN141 |
B | SER261 |
B | ILE500 |
B | MG600 |
B | HOH2060 |
B | HOH2073 |
B | HOH2074 |
site_id | AC8 |
Number of Residues | 19 |
Details | BINDING SITE FOR RESIDUE ADP C 400 |
Chain | Residue |
C | HOH2157 |
C | ILE55 |
C | PRO56 |
C | LYS61 |
C | ASN62 |
C | VAL63 |
C | LYS87 |
C | ALA91 |
C | GLY92 |
C | SER97 |
C | SER98 |
C | SER101 |
C | SER133 |
C | THR183 |
C | HOH2046 |
C | HOH2153 |
C | HOH2154 |
C | HOH2155 |
C | HOH2156 |
site_id | AC9 |
Number of Residues | 23 |
Details | BINDING SITE FOR RESIDUE AGS D 400 |
Chain | Residue |
D | ILE55 |
D | PRO56 |
D | LYS61 |
D | ASN62 |
D | VAL63 |
D | LYS87 |
D | ALA91 |
D | GLY92 |
D | GLY94 |
D | LEU95 |
D | GLY96 |
D | SER97 |
D | SER98 |
D | SER101 |
D | SER133 |
D | ASN141 |
D | THR183 |
D | SER261 |
D | ILE500 |
D | HOH2035 |
D | HOH2103 |
D | HOH2104 |
D | HOH2105 |
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 | 4 |
Details | BINDING: BINDING => ECO:0000255 |
Chain | Residue | Details |
A | LYS90 | |
B | LYS90 | |
C | LYS90 | |
D | LYS90 |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 1 |
Details | Annotated By Reference To The Literature 1fwk |
Chain | Residue | Details |
A | THR183 |
site_id | CSA2 |
Number of Residues | 1 |
Details | Annotated By Reference To The Literature 1fwk |
Chain | Residue | Details |
B | THR183 |
site_id | CSA3 |
Number of Residues | 1 |
Details | Annotated By Reference To The Literature 1fwk |
Chain | Residue | Details |
C | THR183 |
site_id | CSA4 |
Number of Residues | 1 |
Details | Annotated By Reference To The Literature 1fwk |
Chain | Residue | Details |
D | 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 |