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2WOC

Crystal Structure of the dinitrogenase reductase-activating glycohydrolase (DRAG) from Rhodospirillum rubrum

Functional Information from GO Data
ChainGOidnamespacecontents
A0005737cellular_componentcytoplasm
A0009399biological_processnitrogen fixation
A0016787molecular_functionhydrolase activity
A0046872molecular_functionmetal ion binding
A0047407molecular_functionADP-ribosyl-[dinitrogen reductase] hydrolase activity
A0051725biological_processprotein de-ADP-ribosylation
B0005737cellular_componentcytoplasm
B0009399biological_processnitrogen fixation
B0016787molecular_functionhydrolase activity
B0046872molecular_functionmetal ion binding
B0047407molecular_functionADP-ribosyl-[dinitrogen reductase] hydrolase activity
B0051725biological_processprotein de-ADP-ribosylation
C0005737cellular_componentcytoplasm
C0009399biological_processnitrogen fixation
C0016787molecular_functionhydrolase activity
C0046872molecular_functionmetal ion binding
C0047407molecular_functionADP-ribosyl-[dinitrogen reductase] hydrolase activity
C0051725biological_processprotein de-ADP-ribosylation
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MN A 400
ChainResidue
AASP243
AASP245
ATHR246
AFMT402
AHOH2012

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MN A 401
ChainResidue
AASP245
AGLU28
ATHR59
AASP60
AASP97

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE FMT A 402
ChainResidue
AASP60
AASN126
AMET130
AASP245
ATHR246
AMN400

site_idAC4
Number of Residues7
DetailsBINDING SITE FOR RESIDUE GOL A 500
ChainResidue
ASER270
ALYS271
ALEU272
AASP273
AMET274
AHOH2031
CGLN208

site_idAC5
Number of Residues1
DetailsBINDING SITE FOR RESIDUE CL A 501
ChainResidue
AMET45

site_idAC6
Number of Residues7
DetailsBINDING SITE FOR RESIDUE GOL A 502
ChainResidue
AARG43
ALYS44
ALYS231
APRO265
AGLY267
ATRP268
AHOH2145

site_idAC7
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MN B 400
ChainResidue
BASP243
BASP245
BTHR246
BFMT402
BHOH2013

site_idAC8
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MN B 401
ChainResidue
BGLU28
BTHR59
BASP60
BASP97
BASP245

site_idAC9
Number of Residues7
DetailsBINDING SITE FOR RESIDUE FMT B 402
ChainResidue
BASP60
BASN126
BMET130
BASP243
BTHR246
BMN400
BHOH2125

site_idBC1
Number of Residues8
DetailsBINDING SITE FOR RESIDUE GOL B 500
ChainResidue
BALA165
BARG172
BARG192
BLEU193
BGLN196
BHIS197
BHOH2090
BHOH2126

site_idBC2
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CL B 501
ChainResidue
BMET45
BLYS271
BGOL502

site_idBC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE GOL B 502
ChainResidue
BARG43
BGLY267
BTRP268
BCL501

site_idBC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MN C 400
ChainResidue
CASP243
CASP245
CTHR246
CFMT402
CHOH2101

site_idBC5
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MN C 401
ChainResidue
CGLU28
CTHR59
CASP60
CASP97
CASP245

site_idBC6
Number of Residues7
DetailsBINDING SITE FOR RESIDUE FMT C 402
ChainResidue
CASP60
CASN126
CMET130
CASP243
CASP245
CTHR246
CMN400

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues18
DetailsBINDING: BINDING => ECO:0000269|PubMed:19706507
ChainResidueDetails
AASN100
BTYR212
BASP243
BTHR246
CASN100
CGLU121
CHIS158
CTYR212
CASP243
CTHR246
AGLU121
AHIS158
ATYR212
AASP243
ATHR246
BASN100
BGLU121
BHIS158

site_idSWS_FT_FI2
Number of Residues3
DetailsBINDING: BINDING => ECO:0000305|PubMed:19706507
ChainResidueDetails
AASP245
BASP245
CASP245

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PDB entries from 2024-10-09

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