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3HSZ

Crystal structure of E. coli HPPK(F123A)

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 Residues4
DetailsBINDING SITE FOR RESIDUE CL A 191
ChainResidue
APRO114
ALYS119
APRO138
AASP139

site_idAC2
Number of Residues10
DetailsBINDING SITE FOR RESIDUE TRS A 192
ChainResidue
AHIS115
ATRS193
AHOH204
AHOH263
AHOH375
ALEU70
AASP97
AILE98
ALEU111
ATHR112

site_idAC3
Number of Residues11
DetailsBINDING SITE FOR RESIDUE TRS A 193
ChainResidue
AGLU77
AARG92
AASP95
ALEU96
AASP97
AHIS148
ATRS192
AHOH302
AHOH318
AHOH351
AHOH412

site_idAC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ACT A 194
ChainResidue
ALEU11
AALA12
ASER13
APRO14

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

221716

PDB entries from 2024-06-26

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