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3HT0

Crystal structure of E. coli HPPK(F123A) in complex with MgAMPCPP

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
AAPC171
AHOH201
AHOH202

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MG A 162
ChainResidue
AAPC171
AHOH203
AHOH204
AASP95
AASP97
AMG161

site_idAC3
Number of Residues30
DetailsBINDING SITE FOR RESIDUE APC A 171
ChainResidue
ALYS23
ALEU70
AGLN74
AARG92
AASP95
AASP97
AILE98
AARG110
ALEU111
ATHR112
AHIS115
ATYR116
AARG121
AHIS148
AMG161
AMG162
AHOH201
AHOH202
AHOH208
AHOH210
AHOH212
AHOH265
AHOH313
AHOH318
AHOH321
AHOH375
AHOH379
AHOH418
AHOH459
AHOH461

site_idAC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CL A 191
ChainResidue
AARG84
ATRP89
ALYS157
AHOH290

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

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PDB entries from 2024-10-30

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