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7KDR

Crystal structure of Escherichia coli HPPK in complex with bisubstrate inhibitor HP-75

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 Residues28
Detailsbinding site for residue J1L A 201
ChainResidue
ATHR42
AASP95
AASP97
AILE98
AARG110
ALEU111
ATHR112
AHIS115
ATYR116
AARG121
APHE123
APRO43
AEDO203
AEDO204
AHOH327
AHOH335
AHOH360
AHOH368
AHOH388
AHOH423
AHOH440
ALEU45
AGLN48
ATYR53
AASN55
AGLN74
ATRP89
AARG92

site_idAC2
Number of Residues4
Detailsbinding site for residue CL A 202
ChainResidue
ALYS119
APRO138
AASP139
AHOH529

site_idAC3
Number of Residues7
Detailsbinding site for residue EDO A 203
ChainResidue
AGLN48
AARG88
ATYR116
AJ1L201
AHOH305
AHOH313
AHOH348

site_idAC4
Number of Residues6
Detailsbinding site for residue EDO A 204
ChainResidue
AALA6
AASN55
AASP95
AASP97
AJ1L201
AHOH337

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 2024-07-31

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