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1H73

CRYSTAL STRUCTURE OF HOMOSERINE KINASE COMPLEXED WITH THREONINE

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0004413molecular_functionhomoserine kinase activity
A0005524molecular_functionATP binding
A0005737cellular_componentcytoplasm
A0006566biological_processL-threonine metabolic process
A0008652biological_processamino acid biosynthetic process
A0009088biological_processL-threonine biosynthetic process
A0016301molecular_functionkinase activity
A0016740molecular_functiontransferase activity
Functional Information from PDB Data
site_idAC1
Number of Residues12
DetailsBINDING SITE FOR RESIDUE THR A 401
ChainResidue
AALA16
AGLY260
ASER261
AANP418
AASN17
APHE22
AASP23
AASP140
AASN141
ATHR183
AARG187
AARG235

site_idAC2
Number of Residues20
DetailsBINDING SITE FOR RESIDUE ANP A 418
ChainResidue
AILE55
APRO56
ALYS61
AASN62
AVAL63
ALYS87
AALA91
AGLY92
AGLY94
ALEU95
AGLY96
ASER97
ASER98
ASER101
ATHR183
ASER261
ATHR401
AHOH2247
AHOH2248
AHOH2249

Functional Information from PROSITE/UniProt
site_idPS00627
Number of Residues12
DetailsGHMP_KINASES_ATP GHMP kinases putative ATP-binding domain. VKaGsGLGSSAA
ChainResidueDetails
AVAL89-ALA100

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues10
DetailsBinding site: {"evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues1
DetailsAnnotated By Reference To The Literature 1fwk
ChainResidueDetails
ATHR183

site_idMCSA1
Number of Residues2
DetailsM-CSA 778
ChainResidueDetails
AGLU130metal ligand
ATHR183electrostatic stabiliser, polar interaction

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PDB entries from 2026-02-18

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