Loading
PDBj
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDBDonate
RCSB PDBPDBeBMRBAdv. SearchSearch help

1MRR

SUBSTITUTION OF MANGANESE FOR IRON IN RIBONUCLEOTIDE REDUCTASE FROM ESCHERICHIA COLI. SPECTROSCOPIC AND CRYSTALLOGRAPHIC CHARACTERIZATION

Functional Information from GO Data
ChainGOidnamespacecontents
A0004748molecular_functionribonucleoside-diphosphate reductase activity, thioredoxin disulfide as acceptor
A0005506molecular_functioniron ion binding
A0005515molecular_functionprotein binding
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0005971cellular_componentribonucleoside-diphosphate reductase complex
A0009185biological_processribonucleoside diphosphate metabolic process
A0009263biological_processdeoxyribonucleotide biosynthetic process
A0009265biological_process2'-deoxyribonucleotide biosynthetic process
A0015949biological_processnucleobase-containing small molecule interconversion
A0016491molecular_functionoxidoreductase activity
A0042802molecular_functionidentical protein binding
A0046872molecular_functionmetal ion binding
B0004748molecular_functionribonucleoside-diphosphate reductase activity, thioredoxin disulfide as acceptor
B0005506molecular_functioniron ion binding
B0005515molecular_functionprotein binding
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0005971cellular_componentribonucleoside-diphosphate reductase complex
B0009185biological_processribonucleoside diphosphate metabolic process
B0009263biological_processdeoxyribonucleotide biosynthetic process
B0009265biological_process2'-deoxyribonucleotide biosynthetic process
B0015949biological_processnucleobase-containing small molecule interconversion
B0016491molecular_functionoxidoreductase activity
B0042802molecular_functionidentical protein binding
B0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MN A 401
ChainResidue
AASP84
AGLU115
AHIS118
AGLU238
AHOH521

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MN A 402
ChainResidue
AHOH521
AGLU115
AGLU204
AGLU238
AHIS241

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MN B 403
ChainResidue
BASP84
BGLU115
BHIS118
BGLU238
BMN404
BHOH640

site_idAC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MN B 404
ChainResidue
BGLU115
BGLU204
BGLU238
BHIS241
BMN403
BHOH640

site_idAC5
Number of Residues4
DetailsBINDING SITE FOR RESIDUE HG A 405
ChainResidue
ATYR156
ACYS196
AHG412
AHOH520

site_idAC6
Number of Residues5
DetailsBINDING SITE FOR RESIDUE HG B 406
ChainResidue
BTYR156
BCYS196
BVAL200
BHG413
BHOH537

site_idAC7
Number of Residues5
DetailsBINDING SITE FOR RESIDUE HG A 407
ChainResidue
ATYR194
AMET198
AALA265
ACYS272
AHOH524

site_idAC8
Number of Residues4
DetailsBINDING SITE FOR RESIDUE HG B 408
ChainResidue
BVAL210
BCYS214
BLEU304
BHG411

site_idAC9
Number of Residues4
DetailsBINDING SITE FOR RESIDUE HG A 409
ChainResidue
AVAL210
ACYS214
ALEU304
AHOH516

site_idBC1
Number of Residues2
DetailsBINDING SITE FOR RESIDUE HG B 410
ChainResidue
BTYR194
BALA265

site_idBC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE HG B 411
ChainResidue
BASN76
BVAL210
BCYS214
BHG408

site_idBC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE HG A 412
ChainResidue
ATYR157
ACYS196
AVAL200
AHG405

site_idBC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE HG B 413
ChainResidue
BTYR157
BCYS196
BVAL200
BHG406

site_idBC5
Number of Residues3
DetailsBINDING SITE FOR RESIDUE HG B 414
ChainResidue
BTYR194
BCYS268
BCYS272

site_idBC6
Number of Residues4
DetailsBINDING SITE FOR RESIDUE HG A 415
ChainResidue
ALYS284
ACYS305
AGLU309
AHOH554

site_idBC7
Number of Residues3
DetailsBINDING SITE FOR RESIDUE HG B 416
ChainResidue
BCYS214
BPHE218
BHOH562

site_idBC8
Number of Residues4
DetailsBINDING SITE FOR RESIDUE HG B 417
ChainResidue
BMET198
BCYS272
BLEU275
BPHE276

Functional Information from PROSITE/UniProt
site_idPS00368
Number of Residues17
DetailsRIBORED_SMALL Ribonucleotide reductase small subunit signature. SEt.IHSrSYthIirnIV
ChainResidueDetails
ASER114-VAL130

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsActive site: {}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues12
DetailsBinding site: {}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues1
DetailsAnnotated By Reference To The Literature 1xik
ChainResidueDetails
ATYR122

site_idCSA2
Number of Residues1
DetailsAnnotated By Reference To The Literature 1xik
ChainResidueDetails
BTYR122

site_idMCSA1
Number of Residues2
DetailsM-CSA 918
ChainResidueDetails
ATYR122pi-pi interaction, single electron relay
AASP237

site_idMCSA2
Number of Residues2
DetailsM-CSA 918
ChainResidueDetails
BTYR122pi-pi interaction, single electron relay
BASP237

246704

PDB entries from 2025-12-24

PDB statisticsPDBj update infoContact PDBjnumon