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2VD3

The structure of histidine inhibited HisG from Methanobacterium thermoautotrophicum

Functional Information from GO Data
ChainGOidnamespacecontents
A0000105biological_processhistidine biosynthetic process
A0000166molecular_functionnucleotide binding
A0000287molecular_functionmagnesium ion binding
A0003879molecular_functionATP phosphoribosyltransferase activity
A0005524molecular_functionATP binding
A0005737cellular_componentcytoplasm
A0008652biological_processamino acid biosynthetic process
A0016740molecular_functiontransferase activity
A0016757molecular_functionglycosyltransferase activity
A0046872molecular_functionmetal ion binding
B0000105biological_processhistidine biosynthetic process
B0000166molecular_functionnucleotide binding
B0000287molecular_functionmagnesium ion binding
B0003879molecular_functionATP phosphoribosyltransferase activity
B0005524molecular_functionATP binding
B0005737cellular_componentcytoplasm
B0008652biological_processamino acid biosynthetic process
B0016740molecular_functiontransferase activity
B0016757molecular_functionglycosyltransferase activity
B0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues1
DetailsBINDING SITE FOR RESIDUE CL A1007
ChainResidue
ASER160

site_idAC2
Number of Residues3
DetailsBINDING SITE FOR RESIDUE IMD A1288
ChainResidue
AGLU125
AASP134
AALA135

site_idAC3
Number of Residues2
DetailsBINDING SITE FOR RESIDUE IMD A1289
ChainResidue
ALYS260
AHOH2009

site_idAC4
Number of Residues10
DetailsBINDING SITE FOR RESIDUE HIS A1290
ChainResidue
AGLY235
AMET236
ATHR237
AGLY238
ATHR240
AVAL256
AASP276
AMET218
ALEU219
AASN220

site_idAC5
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CL A1291
ChainResidue
APRO1
ALYS194
AGLY196
AILE197

site_idAC6
Number of Residues1
DetailsBINDING SITE FOR RESIDUE CL A1292
ChainResidue
ALYS183

site_idAC7
Number of Residues2
DetailsBINDING SITE FOR RESIDUE CL A1293
ChainResidue
AGLU119
ATHR157

site_idAC8
Number of Residues2
DetailsBINDING SITE FOR RESIDUE MG A1294
ChainResidue
AASP158
ALEU159

site_idAC9
Number of Residues1
DetailsBINDING SITE FOR RESIDUE MG A1295
ChainResidue
AGLU82

site_idBC1
Number of Residues3
DetailsBINDING SITE FOR RESIDUE MG A1296
ChainResidue
AGLU22
AGLY27
AGLN41

site_idBC2
Number of Residues1
DetailsBINDING SITE FOR RESIDUE MG A1297
ChainResidue
AASP175

site_idBC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE MPD A1298
ChainResidue
AGLU119
AGLU139
ALEU140
ATHR141

site_idBC4
Number of Residues3
DetailsBINDING SITE FOR RESIDUE MRD A1299
ChainResidue
AGLY151
AVAL152
AASP154

site_idBC5
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MPD A1300
ChainResidue
AARG4
AGLU46
AALA63
AASP65
ALYS194

site_idBC6
Number of Residues2
DetailsBINDING SITE FOR RESIDUE MG B1118
ChainResidue
AASP61
BGLU136

site_idBC7
Number of Residues3
DetailsBINDING SITE FOR RESIDUE IMD B1288
ChainResidue
BLYS88
BASP109
BASP258

site_idBC8
Number of Residues2
DetailsBINDING SITE FOR RESIDUE CL B1289
ChainResidue
BGLU119
BTHR157

site_idBC9
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CL B1290
ChainResidue
BPRO1
BGLY196
BILE197

site_idCC1
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CL B1291
ChainResidue
BLEU171
BARG172
BVAL173

site_idCC2
Number of Residues2
DetailsBINDING SITE FOR RESIDUE CL B1292
ChainResidue
BALA52
BALA53

site_idCC3
Number of Residues3
DetailsBINDING SITE FOR RESIDUE MG B1293
ChainResidue
BLYS10
BARG51
BALA52

site_idCC4
Number of Residues2
DetailsBINDING SITE FOR RESIDUE MG B1294
ChainResidue
BGLU145
BASP158

site_idCC5
Number of Residues4
DetailsBINDING SITE FOR RESIDUE MG B1295
ChainResidue
BGLY11
BARG12
BSER14
BGLU15

site_idCC6
Number of Residues3
DetailsBINDING SITE FOR RESIDUE MG B1296
ChainResidue
BSER9
BHOH2001
BHOH2006

site_idCC7
Number of Residues4
DetailsBINDING SITE FOR RESIDUE MPD B1297
ChainResidue
BGLU119
BGLU139
BLEU140
BTHR141

site_idCC8
Number of Residues4
DetailsBINDING SITE FOR RESIDUE MPD B1298
ChainResidue
BLYS2
BARG4
BALA63
BASP65

site_idCC9
Number of Residues4
DetailsBINDING SITE FOR RESIDUE MPD B1299
ChainResidue
BSER93
BSER160
BSER161
BGLY163

site_idDC1
Number of Residues11
DetailsBINDING SITE FOR RESIDUE HIS B1300
ChainResidue
BLEU219
BASN220
BGLY235
BMET236
BTHR237
BGLY238
BTHR240
BALA255
BVAL256
BASP276
BHOH2022

Functional Information from PROSITE/UniProt
site_idPS01316
Number of Residues22
DetailsATP_P_PHORIBOSYLTR ATP phosphoribosyltransferase signature. EiapfiGvAdlItDLssTGtTL
ChainResidueDetails
AGLU145-LEU166

218853

PDB entries from 2024-04-24

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