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6MV9

X-ray crystal structure of Bacillus subtilis ribonucleotide reductase NrdE alpha subunit with TTP and ADP

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0003824molecular_functioncatalytic activity
A0004748molecular_functionribonucleoside-diphosphate reductase activity, thioredoxin disulfide as acceptor
A0005524molecular_functionATP binding
A0005971cellular_componentribonucleoside-diphosphate reductase complex
A0009263biological_processdeoxyribonucleotide biosynthetic process
A0016491molecular_functionoxidoreductase activity
B0000166molecular_functionnucleotide binding
B0003824molecular_functioncatalytic activity
B0004748molecular_functionribonucleoside-diphosphate reductase activity, thioredoxin disulfide as acceptor
B0005524molecular_functionATP binding
B0005971cellular_componentribonucleoside-diphosphate reductase complex
B0009263biological_processdeoxyribonucleotide biosynthetic process
B0016491molecular_functionoxidoreductase activity
Functional Information from PDB Data
site_idAC1
Number of Residues13
Detailsbinding site for residue TTP A 801
ChainResidue
AASP177
AMG803
BLYS194
BTYR236
BALA237
ASER178
ALEU179
AILE182
AARG207
AILE213
ALYS214
ATHR220
ALYS221

site_idAC2
Number of Residues7
Detailsbinding site for residue ADP A 802
ChainResidue
AVAL33
AHIS34
APHE37
AASN42
APHE89
AARG90
APHE91

site_idAC3
Number of Residues1
Detailsbinding site for residue MG A 803
ChainResidue
ATTP801

site_idAC4
Number of Residues13
Detailsbinding site for residue TTP B 801
ChainResidue
ALYS194
ATYR236
AALA237
BASP177
BSER178
BLEU179
BILE182
BARG207
BILE213
BLYS214
BTHR220
BLYS221
BMG803

site_idAC5
Number of Residues5
Detailsbinding site for residue ADP B 802
ChainResidue
BHIS34
BPHE37
BASN42
BARG90
BPHE91

site_idAC6
Number of Residues1
Detailsbinding site for residue MG B 803
ChainResidue
BTTP801

Functional Information from PROSITE/UniProt
site_idPS00089
Number of Residues23
DetailsRIBORED_LARGE Ribonucleotide reductase large subunit signature. WkkLkafvaehGMYHsyrLCiaP
ChainResidueDetails
ATRP558-PRO580

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsActive site: {"description":"Proton acceptor","evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues2
DetailsActive site: {"description":"Cysteine radical intermediate","evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues22
DetailsBinding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues4
DetailsSite: {"description":"Important for hydrogen atom transfer","evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues4
DetailsSite: {"description":"Allosteric effector binding","evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues4
DetailsSite: {"description":"Important for electron transfer","evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues4
DetailsSite: {"description":"Interacts with thioredoxin/glutaredoxin","evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

238582

PDB entries from 2025-07-09

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