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3HSD

Crystal structure of E. coli HPPK(Y53A)

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
B0000287molecular_functionmagnesium ion binding
B0003848molecular_function2-amino-4-hydroxy-6-hydroxymethyldihydropteridine diphosphokinase activity
B0005524molecular_functionATP binding
B0009396biological_processfolic acid-containing compound biosynthetic process
B0016301molecular_functionkinase activity
B0046654biological_processtetrahydrofolate biosynthetic process
B0046656biological_processfolic acid biosynthetic process
Functional Information from PDB Data
site_idAC1
Number of Residues7
DetailsBINDING SITE FOR RESIDUE MG A 161
ChainResidue
AASP95
AASP97
AMG162
AHOH201
AHOH202
AHOH203
AHOH204

site_idAC2
Number of Residues7
DetailsBINDING SITE FOR RESIDUE MG A 162
ChainResidue
AMG161
AHOH204
AHOH205
AHOH206
AHOH207
AASP95
AASP97

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MG A 163
ChainResidue
AHOH214
AHOH215
AHOH218
AHOH219
BHOH216
BHOH217

site_idAC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CL A 191
ChainResidue
APRO114
ALYS119
APRO138
AASP139
AHOH456

site_idAC5
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CL A 192
ChainResidue
ATRP158
BHOH265
BHOH277

site_idAC6
Number of Residues2
DetailsBINDING SITE FOR RESIDUE GOL A 193
ChainResidue
AHIS148
AHOH249

site_idAC7
Number of Residues6
DetailsBINDING SITE FOR RESIDUE GOL A 194
ChainResidue
AALA53
AASN55
AARG92
APHE123
AHOH512
BLYS23

site_idAC8
Number of Residues7
DetailsBINDING SITE FOR RESIDUE GOL A 159
ChainResidue
AASN19
APHE39
AHOH230
AHOH260
BTRP89
BGLY90
BHOH225

site_idAC9
Number of Residues7
DetailsBINDING SITE FOR RESIDUE MG B 161
ChainResidue
AHOH211
BASP95
BASP97
BMG162
BHOH208
BHOH209
BHOH210

site_idBC1
Number of Residues7
DetailsBINDING SITE FOR RESIDUE MG B 162
ChainResidue
AGLU16
AHOH211
AHOH212
BASP95
BASP97
BMG161
BHOH213

site_idBC2
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CL B 191
ChainResidue
AHOH493
BLYS119
BASP139

site_idBC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE GOL B 192
ChainResidue
BGLU30
BSER63
BGLU68
BHOH534
BHOH548

site_idBC4
Number of Residues7
DetailsBINDING SITE FOR RESIDUE GOL B 193
ChainResidue
BGLU77
BLEU78
BGLY81
BARG82
BARG92
BTHR93
BLEU94

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

site_idMCSA2
Number of Residues4
DetailsM-CSA 151
ChainResidueDetails
BARG82electrostatic stabiliser, hydrogen bond donor
BARG92electrostatic stabiliser, hydrogen bond donor
BASP95metal ligand
BASP97metal ligand

220113

PDB entries from 2024-05-22

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