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7MMR

Crystal Structure of the Class Ie Ribonucleotide Reductase Beta-NrdI complex from Aerococcus urinae in Oxidized Form with Cu(I) bound

Functional Information from GO Data
ChainGOidnamespacecontents
A0004748molecular_functionribonucleoside-diphosphate reductase activity, thioredoxin disulfide as acceptor
A0005971cellular_componentribonucleoside-diphosphate reductase complex
A0009263biological_processdeoxyribonucleotide biosynthetic process
A0016020cellular_componentmembrane
A0016491molecular_functionoxidoreductase activity
A0046872molecular_functionmetal ion binding
B0004748molecular_functionribonucleoside-diphosphate reductase activity, thioredoxin disulfide as acceptor
B0005971cellular_componentribonucleoside-diphosphate reductase complex
B0009263biological_processdeoxyribonucleotide biosynthetic process
B0016020cellular_componentmembrane
B0016491molecular_functionoxidoreductase activity
B0046872molecular_functionmetal ion binding
C0004748molecular_functionribonucleoside-diphosphate reductase activity, thioredoxin disulfide as acceptor
C0005971cellular_componentribonucleoside-diphosphate reductase complex
C0009263biological_processdeoxyribonucleotide biosynthetic process
C0016020cellular_componentmembrane
C0016491molecular_functionoxidoreductase activity
C0046872molecular_functionmetal ion binding
D0004748molecular_functionribonucleoside-diphosphate reductase activity, thioredoxin disulfide as acceptor
D0005971cellular_componentribonucleoside-diphosphate reductase complex
D0009263biological_processdeoxyribonucleotide biosynthetic process
D0016020cellular_componentmembrane
D0016491molecular_functionoxidoreductase activity
D0046872molecular_functionmetal ion binding
E0000166molecular_functionnucleotide binding
E0010181molecular_functionFMN binding
E0036211biological_processprotein modification process
F0000166molecular_functionnucleotide binding
F0010181molecular_functionFMN binding
F0036211biological_processprotein modification process
G0000166molecular_functionnucleotide binding
G0010181molecular_functionFMN binding
G0036211biological_processprotein modification process
H0000166molecular_functionnucleotide binding
H0010181molecular_functionFMN binding
H0036211biological_processprotein modification process
Functional Information from PDB Data
site_idAC1
Number of Residues5
Detailsbinding site for residue CU1 A 401
ChainResidue
AVAL116
APRO176
AHIS213
AHOH553
AHOH597

site_idAC2
Number of Residues3
Detailsbinding site for residue CU1 A 402
ChainResidue
ATHR75
ACYS131
AGLN135

site_idAC3
Number of Residues6
Detailsbinding site for residue GOL A 403
ChainResidue
AASN42
AARG43
ETYR50
EGLY52
EFMN201
AGLU39

site_idAC4
Number of Residues5
Detailsbinding site for residue CU1 B 401
ChainResidue
BVAL116
BPRO176
BHIS213
BHOH550
BHOH586

site_idAC5
Number of Residues3
Detailsbinding site for residue CU1 B 402
ChainResidue
BTHR75
BCYS131
BGLN135

site_idAC6
Number of Residues6
Detailsbinding site for residue GOL B 403
ChainResidue
BTYR6
BSER11
BARG25
BSER100
BLEU101
BGLN106

site_idAC7
Number of Residues6
Detailsbinding site for residue GOL B 404
ChainResidue
BTRP63
BASN64
BGLN71
BLEU130
BCYS131
BGLN135

site_idAC8
Number of Residues4
Detailsbinding site for residue CU1 C 401
ChainResidue
CVAL116
CHIS213
CHOH571
CHOH594

site_idAC9
Number of Residues1
Detailsbinding site for residue CU1 C 402
ChainResidue
CHIS256

site_idAD1
Number of Residues7
Detailsbinding site for residue GOL C 403
ChainResidue
CTYR6
CSER11
CARG25
CSER100
CLEU101
CGLN106
CHOH504

site_idAD2
Number of Residues6
Detailsbinding site for residue TRS C 404
ChainResidue
CTRP63
CASN64
CGLN71
CLEU130
CTHR132
CGLN135

site_idAD3
Number of Residues4
Detailsbinding site for residue CU1 C 405
ChainResidue
CTRP63
CTHR75
CCYS131
CGLN135

site_idAD4
Number of Residues1
Detailsbinding site for residue CA C 406
ChainResidue
CGLU299

site_idAD5
Number of Residues3
Detailsbinding site for residue CA C 407
ChainResidue
CGLY263
CASP266
CGLU267

site_idAD6
Number of Residues4
Detailsbinding site for residue CA C 408
ChainResidue
CGLU52
CARG121
DTRP41
DHOH546

site_idAD7
Number of Residues5
Detailsbinding site for residue CU1 D 401
ChainResidue
DVAL116
DPRO176
DHIS213
DHOH563
DHOH597

site_idAD8
Number of Residues3
Detailsbinding site for residue CU1 D 402
ChainResidue
DTHR75
DCYS131
DGLN135

site_idAD9
Number of Residues6
Detailsbinding site for residue GOL D 403
ChainResidue
DTYR6
DSER11
DGLU14
DARG25
DLEU101
DGLU103

site_idAE1
Number of Residues5
Detailsbinding site for residue GOL D 404
ChainResidue
DTRP63
DASN64
DGLN71
DLEU130
DGLN135

site_idAE2
Number of Residues23
Detailsbinding site for residue FMN E 201
ChainResidue
EPHE95
ESER98
EPHE99
EALA100
ELEU120
ECA202
EHOH307
APHE215
AGOL403
ESER9
ETHR10
ESER12
EASN13
EASN14
ETHR15
EPRO48
ETHR49
ETYR50
ESER51
EGLY52
EGLY53
EGLY91
EASN92

site_idAE3
Number of Residues4
Detailsbinding site for residue CA E 202
ChainResidue
AASN282
EASN92
ELEU120
EFMN201

site_idAE4
Number of Residues22
Detailsbinding site for residue FMN G 201
ChainResidue
CPHE215
GSER9
GTHR10
GSER12
GASN13
GASN14
GTHR15
GPRO48
GTHR49
GTYR50
GSER51
GGLY52
GGLY53
GGLY91
GASN92
GPHE95
GSER98
GPHE99
GALA100
GLEU120
GCA202
GHOH310

site_idAE5
Number of Residues4
Detailsbinding site for residue CA G 202
ChainResidue
CASN282
GASN92
GLEU120
GFMN201

site_idAE6
Number of Residues23
Detailsbinding site for residue FMN F 201
ChainResidue
BGLU39
BPHE215
FSER9
FTHR10
FSER12
FASN13
FASN14
FTHR15
FPRO48
FTHR49
FTYR50
FSER51
FGLY52
FGLY53
FGLY91
FASN92
FPHE95
FSER98
FPHE99
FALA100
FLEU120
FCA202
FHOH311

site_idAE7
Number of Residues4
Detailsbinding site for residue CA F 202
ChainResidue
BASN282
FASN92
FLEU120
FFMN201

site_idAE8
Number of Residues23
Detailsbinding site for residue FMN H 201
ChainResidue
DGLU39
DPHE215
HSER9
HTHR10
HSER12
HASN13
HASN14
HTHR15
HPRO48
HTHR49
HTYR50
HSER51
HGLY52
HGLY53
HGLY91
HASN92
HPHE95
HSER98
HPHE99
HALA100
HLEU120
HCA202
HHOH306

site_idAE9
Number of Residues3
Detailsbinding site for residue CA H 202
ChainResidue
HASN92
HLEU120
HFMN201

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PDB entries from 2024-11-06

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