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1TMJ

Crystal structure of E.coli apo-HPPK(W89A) at 1.45 Angstrom resolution

Functional Information from GO Data
ChainGOidnamespacecontents
A0000287molecular_functionmagnesium ion binding
A0003848molecular_function2-amino-4-hydroxy-6-hydroxymethyldihydropteridine diphosphokinase activity
A0005524molecular_functionATP binding
A0009396biological_processfolic acid-containing compound biosynthetic process
A0016301molecular_functionkinase activity
A0016310biological_processphosphorylation
A0046654biological_processtetrahydrofolate biosynthetic process
A0046656biological_processfolic acid biosynthetic process
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MG A 161
ChainResidue
AASP95
AASP97
AMG162
AHOH215
AHOH257
AHOH258

site_idAC2
Number of Residues7
DetailsBINDING SITE FOR RESIDUE MG A 162
ChainResidue
AHOH244
AHOH246
AHOH258
AHOH260
AASP95
AASP97
AMG161

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CL A 163
ChainResidue
APRO114
ALYS119
APHE137
APRO138
AASP139
AHOH337

Functional Information from PROSITE/UniProt
site_idPS00794
Number of Residues12
DetailsHPPK 7,8-dihydro-6-hydroxymethylpterin-pyrophosphokinase signature. RaGPRtlDLDIM
ChainResidueDetails
AARG88-MET99

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1hka
ChainResidueDetails
AARG92
AARG82

site_idMCSA1
Number of Residues4
DetailsM-CSA 151
ChainResidueDetails
AVAL83electrostatic stabiliser, hydrogen bond donor
ATHR93electrostatic stabiliser, hydrogen bond donor
ALEU96metal ligand
AILE98metal ligand

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PDB entries from 2024-10-16

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