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2WOE

Crystal Structure of the D97N variant of dinitrogenase reductase- activating glycohydrolase (DRAG) from Rhodospirillum rubrum in complex with ADP-ribose

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
AGLU28
AASP243
AASP245
ATHR246
AAR6401

site_idAC2
Number of Residues27
DetailsBINDING SITE FOR RESIDUE AR6 A 401
ChainResidue
AASN100
ATHR101
ACYS102
AGLU121
AGLY122
AALA124
AGLY125
AASN126
AGLY127
AHIS158
AALA211
ATYR212
AASP243
AASP245
ATHR246
AMN400
AHOH2203
AHOH2266
AHOH2267
AHOH2268
CLYS54
CASP273
CLYS275
AGLU28
AASP60
AASN97
AGLY99

site_idAC3
Number of Residues13
DetailsBINDING SITE FOR RESIDUE TLA A 500
ChainResidue
AARG43
ALYS231
AHOH2270
AHOH2271
AHOH2272
AHOH2273
AHOH2274
AHOH2275
BGLY3
BPRO4
BARG9
BTHR258
BTYR259

site_idAC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE GOL A 600
ChainResidue
AARG187
AALA190
AASN191
APHE202
AHOH2276
BHIS197

site_idAC5
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MN B 400
ChainResidue
BGLU28
BASP243
BASP245
BTHR246
BAR6401

site_idAC6
Number of Residues23
DetailsBINDING SITE FOR RESIDUE AR6 B 401
ChainResidue
BGLU28
BASP60
BASN97
BGLY99
BASN100
BTHR101
BCYS102
BGLU121
BGLY122
BALA124
BGLY125
BASN126
BGLY127
BHIS158
BTYR212
BASP243
BASP245
BTHR246
BMN400
BHOH2164
BHOH2210
BHOH2275
BHOH2276

site_idAC7
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MN C 400
ChainResidue
CGLU28
CASP243
CASP245
CTHR246
CAR6401

site_idAC8
Number of Residues25
DetailsBINDING SITE FOR RESIDUE AR6 C 401
ChainResidue
CALA211
CTYR212
CASP243
CASP245
CTHR246
CMN400
CHOH2203
CHOH2204
CHOH2205
CHOH2206
BASP273
BLYS275
CASP60
CASN97
CGLY99
CASN100
CTHR101
CCYS102
CGLU121
CGLY122
CALA124
CGLY125
CASN126
CGLY127
CHIS158

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 2024-08-28

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