Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

3IP0

Crystal structure of E. coli HPPK in complex with MgAMPCPP and 6-hydroxymethylpterin/6-carboxypterin

Replaces:  3H4AReplaces:  1F9Y
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 Residues6
DetailsBINDING SITE FOR RESIDUE MG A 161
ChainResidue
AASP95
AASP97
AMG162
AAPC171
AHOH201
AHOH202

site_idAC2
Number of Residues7
DetailsBINDING SITE FOR RESIDUE MG A 162
ChainResidue
AAPC171
AHHR181
AHHS182
AHOH203
AASP95
AASP97
AMG161

site_idAC3
Number of Residues32
DetailsBINDING SITE FOR RESIDUE APC A 171
ChainResidue
AGLN74
AARG82
AARG84
ATRP89
AARG92
AASP95
AASP97
AILE98
AARG110
ALEU111
ATHR112
AHIS115
ATYR116
AARG121
AMG161
AMG162
AHHR181
AHHS182
AACT194
AHOH201
AHOH202
AHOH203
AHOH216
AHOH248
AHOH264
AHOH322
AHOH364
AHOH496
AHOH499
AHOH504
AHOH505
AHOH511

site_idAC4
Number of Residues16
DetailsBINDING SITE FOR RESIDUE HHR A 181
ChainResidue
ATHR42
APRO43
ALEU45
ATYR53
AASN55
ATRP89
AARG92
AASP95
APHE123
AMG162
AAPC171
AHOH203
AHOH219
AHOH243
AHOH298
AHOH504

site_idAC5
Number of Residues18
DetailsBINDING SITE FOR RESIDUE HHS A 182
ChainResidue
ATHR42
APRO43
ALEU45
ATYR53
AASN55
ATRP89
AARG92
AASP95
APHE123
AMG162
AAPC171
AHOH203
AHOH219
AHOH243
AHOH298
AHOH503
AHOH504
AHOH511

site_idAC6
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CL A 191
ChainResidue
AASN107
ALYS119
APHE137
APRO138
AASP139
AHOH486

site_idAC7
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CL A 192
ChainResidue
AHOH206
AHOH206
AHOH222
AHOH222

site_idAC8
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CL A 193
ChainResidue
AHOH324
AHOH324
AHOH453
AHOH453

site_idAC9
Number of Residues5
DetailsBINDING SITE FOR RESIDUE ACT A 194
ChainResidue
ATYR116
AAPC171
AHOH207
AHOH346
AHOH499

site_idBC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE ACT A 195
ChainResidue
ASER31
AHIS32
AHOH382
AHOH402
AGLU30

site_idBC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ACT A 196
ChainResidue
ALYS154
AHOH280
AHOH474
AHOH512

site_idBC3
Number of Residues10
DetailsBINDING SITE FOR RESIDUE ACT A 197
ChainResidue
ALEU11
APRO51
AALA65
APRO66
AHOH257
AHOH284
AHOH308
AHOH353
AHOH369
AHOH515

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_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1hka
ChainResidueDetails
AARG92
AARG82

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

PDB statisticsPDBj update infoContact PDBjnumon