Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

1H72

CRYSTAL STRUCTURE OF HOMOSERINE KINASE COMPLEXED WITH HSE

Functional Information from GO Data
ChainGOidnamespacecontents
C0004413molecular_functionhomoserine kinase activity
C0005524molecular_functionATP binding
C0005737cellular_componentcytoplasm
C0006566biological_processthreonine metabolic process
C0009088biological_processthreonine biosynthetic process
C0016301molecular_functionkinase activity
Functional Information from PDB Data
site_idAC1
Number of Residues8
DetailsBINDING SITE FOR RESIDUE HSE C1300
ChainResidue
CASN17
CASP23
CASP140
CASN141
CARG187
CARG235
CGLY260
CANP1301

site_idAC2
Number of Residues23
DetailsBINDING SITE FOR RESIDUE ANP C1301
ChainResidue
CPRO56
CLYS61
CASN62
CVAL63
CLYS87
CALA91
CGLY92
CGLY94
CLEU95
CGLY96
CSER97
CSER98
CSER101
CSER133
CILE181
CTHR183
CSER261
CHSE1300
CHOH2263
CHOH2303
CHOH2305
CHOH2307
CILE55

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE TRS C1302
ChainResidue
CPRO32
CTYR33
CASP73
CASN76
CHOH2122
CHOH2308

Functional Information from PROSITE/UniProt
site_idPS00627
Number of Residues12
DetailsGHMP_KINASES_ATP GHMP kinases putative ATP-binding domain. VKaGsGLGSSAA
ChainResidueDetails
CVAL89-ALA100

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsBINDING: BINDING => ECO:0000255
ChainResidueDetails
CLYS90

Catalytic Information from CSA
site_idCSA1
Number of Residues1
DetailsAnnotated By Reference To The Literature 1fwk
ChainResidueDetails
CTHR183

site_idMCSA1
Number of Residues2
DetailsM-CSA 778
ChainResidueDetails
CGLU130metal ligand
CTHR183electrostatic stabiliser, polar interaction

222624

PDB entries from 2024-07-17

PDB statisticsPDBj update infoContact PDBjnumon