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1FWK

CRYSTAL STRUCTURE OF HOMOSERINE KINASE COMPLEXED WITH ADP

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0004413molecular_functionhomoserine kinase activity
A0005524molecular_functionATP binding
A0005737cellular_componentcytoplasm
A0006566biological_processthreonine metabolic process
A0008652biological_processamino acid biosynthetic process
A0009088biological_processthreonine biosynthetic process
A0016301molecular_functionkinase activity
A0016740molecular_functiontransferase activity
B0000166molecular_functionnucleotide binding
B0004413molecular_functionhomoserine kinase activity
B0005524molecular_functionATP binding
B0005737cellular_componentcytoplasm
B0006566biological_processthreonine metabolic process
B0008652biological_processamino acid biosynthetic process
B0009088biological_processthreonine biosynthetic process
B0016301molecular_functionkinase activity
B0016740molecular_functiontransferase activity
C0000166molecular_functionnucleotide binding
C0004413molecular_functionhomoserine kinase activity
C0005524molecular_functionATP binding
C0005737cellular_componentcytoplasm
C0006566biological_processthreonine metabolic process
C0008652biological_processamino acid biosynthetic process
C0009088biological_processthreonine biosynthetic process
C0016301molecular_functionkinase activity
C0016740molecular_functiontransferase activity
D0000166molecular_functionnucleotide binding
D0004413molecular_functionhomoserine kinase activity
D0005524molecular_functionATP binding
D0005737cellular_componentcytoplasm
D0006566biological_processthreonine metabolic process
D0008652biological_processamino acid biosynthetic process
D0009088biological_processthreonine biosynthetic process
D0016301molecular_functionkinase activity
D0016740molecular_functiontransferase activity
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MG D 597
ChainResidue
DSER98
DSER134
DADP900
DHOH996
DHOH1007

site_idAC2
Number of Residues19
DetailsBINDING SITE FOR RESIDUE ADP A 600
ChainResidue
ALYS87
AALA91
AGLY92
AGLY96
ASER97
ASER98
ASER101
ASER133
ATHR183
AHOH604
AHOH615
AHOH616
AHOH630
AHOH642
AHOH726
APRO56
ALYS61
AASN62
AVAL63

site_idAC3
Number of Residues14
DetailsBINDING SITE FOR RESIDUE ADP B 700
ChainResidue
BPRO56
BASN62
BVAL63
BALA91
BGLY92
BSER97
BSER98
BSER101
BTHR183
BHOH709
BHOH717
BHOH728
BHOH729
BHOH801

site_idAC4
Number of Residues18
DetailsBINDING SITE FOR RESIDUE ADP C 800
ChainResidue
CILE55
CLYS61
CASN62
CVAL63
CLYS87
CALA91
CGLY92
CSER97
CSER98
CSER101
CSER133
CHOH806
CHOH830
CHOH834
CHOH852
CHOH905
CHOH951
CHOH967

site_idAC5
Number of Residues19
DetailsBINDING SITE FOR RESIDUE ADP D 900
ChainResidue
DASN54
DILE55
DPRO56
DLYS61
DASN62
DVAL63
DLYS87
DALA91
DGLY92
DSER97
DSER98
DSER101
DSER133
DTHR183
DMG597
DHOH903
DHOH914
DHOH927
DHOH1042

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 Residues40
DetailsBinding site: {"evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues1
Detailsa catalytic site defined by CSA, PubMed 11535056
ChainResidueDetails
DTHR183

site_idCSA2
Number of Residues1
Detailsa catalytic site defined by CSA, PubMed 11535056
ChainResidueDetails
ATHR183

site_idCSA3
Number of Residues1
Detailsa catalytic site defined by CSA, PubMed 11535056
ChainResidueDetails
BTHR183

site_idCSA4
Number of Residues1
Detailsa catalytic site defined by CSA, PubMed 11535056
ChainResidueDetails
CTHR183

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

site_idMCSA2
Number of Residues2
DetailsM-CSA 778
ChainResidueDetails
BGLU130metal ligand
BTHR183electrostatic stabiliser, polar interaction

site_idMCSA3
Number of Residues2
DetailsM-CSA 778
ChainResidueDetails
CGLU130metal ligand
CTHR183electrostatic stabiliser, polar interaction

site_idMCSA4
Number of Residues2
DetailsM-CSA 778
ChainResidueDetails
DGLU130metal ligand
DTHR183electrostatic stabiliser, polar interaction

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PDB entries from 2025-07-23

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