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3HSJ

Crystal structure of E. coli HPPK(N55A)

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
A0046654biological_processtetrahydrofolate biosynthetic process
A0046656biological_processfolic acid biosynthetic process
Functional Information from PDB Data
site_idAC1
Number of Residues7
DetailsBINDING SITE FOR RESIDUE ACT A 191
ChainResidue
AALA132
APRO133
AGLU134
AGOL195
AHOH299
AHOH370
AHOH422

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE ACT A 192
ChainResidue
AHIS32
AHOH224
AHOH332
AGLU30
ASER31

site_idAC3
Number of Residues3
DetailsBINDING SITE FOR RESIDUE ACT A 193
ChainResidue
ALEU11
APRO14
AHOH320

site_idAC4
Number of Residues3
DetailsBINDING SITE FOR RESIDUE GOL A 194
ChainResidue
ATYR53
APHE123
AHOH284

site_idAC5
Number of Residues5
DetailsBINDING SITE FOR RESIDUE GOL A 195
ChainResidue
ATYR4
ALEU34
AILE131
AACT191
AHOH433

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

Catalytic Information from CSA
site_idMCSA1
Number of Residues4
DetailsM-CSA 151
ChainResidueDetails
AARG82electrostatic stabiliser, hydrogen bond donor
AARG92electrostatic stabiliser, hydrogen bond donor
AASP95metal ligand
AASP97metal ligand

219140

PDB entries from 2024-05-01

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