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LOCUS 1MRR_A 375 aa linear BCT 10-OCT-2012
DEFINITION Chain A, Substitution Of Manganese For Iron In Ribonucleotide
Reductase From Escherichia Coli. Spectroscopic And Crystallographic
Characterization.
ACCESSION 1MRR_A
VERSION 1MRR_A GI:494379
DBSOURCE pdb: molecule 1MRR, chain 65, release Aug 28, 2012;
deposition: Jul 28, 1992;
class: Reductase(Acting On Ch2);
source: Mmdb_id: 50351, Pdb_id 1: 1MRR;
Exp. method: X-Ray Diffraction.
KEYWORDS .
SOURCE Escherichia coli
ORGANISM Escherichia coli
Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
Enterobacteriaceae; Escherichia.
REFERENCE 1 (residues 1 to 375)
AUTHORS Nordlund,P., Sjoberg,B.M. and Eklund,H.
TITLE Three-dimensional structure of the free radical protein of
ribonucleotide reductase
JOURNAL Nature 345 (6276), 593-598 (1990)
PUBMED 2190093
REFERENCE 2 (residues 1 to 375)
AUTHORS Atta,M., Nordlund,P., Aberg,A., Eklund,H. and Fontecave,M.
TITLE Substitution of manganese for iron in ribonucleotide reductase from
Escherichia coli. Spectroscopic and crystallographic
characterization
JOURNAL J. Biol. Chem. 267 (29), 20682-20688 (1992)
PUBMED 1328209
REFERENCE 3 (residues 1 to 375)
AUTHORS Eklund,H. and Nordlund,P.
TITLE Direct Submission
JOURNAL Submitted (28-JUL-1992)
COMMENT 1 Ribonucleotide Reductase R1 Protein.
FEATURES Location/Qualifiers
source 1..375
/organism="Escherichia coli"
/db_xref="taxon:562"
Region 28..340
/region_name="RNRR2"
/note="Ribonucleotide Reductase, R2/beta subunit,
ferritin-like diiron-binding domain; cd01049"
/db_xref="CDD:153108"
SecStr 35..46
/sec_str_type="helix"
/note="helix 1"
Site order(37,44,109..110,113,116..117,120,123,137..138,141)
/site_type="other"
/note="dimer interface [polypeptide binding]"
/db_xref="CDD:153108"
Site order(48,84,115,118,122,236..237,241)
/site_type="other"
/note="putative radical transfer pathway"
/db_xref="CDD:153108"
SecStr 57..65
/sec_str_type="helix"
/note="helix 2"
SecStr 67..87
/sec_str_type="helix"
/note="helix 3"
Site order(84,115,118,204,238,241)
/site_type="other"
/note="diiron center [ion binding]"
/db_xref="CDD:153108"
Het join(bond(84),bond(115),bond(118),bond(238))
/heterogen="( MN,1000 )"
SecStr 102..129
/sec_str_type="helix"
/note="helix 4"
Het join(bond(115),bond(204),bond(238),bond(241))
/heterogen="( MN,1001 )"
Site 122
/site_type="other"
/note="tyrosyl radical"
/db_xref="CDD:153108"
SecStr 133..140
/sec_str_type="helix"
/note="helix 5"
SecStr 143..151
/sec_str_type="helix"
/note="helix 6"
SecStr 153..169
/sec_str_type="helix"
/note="helix 7"
SecStr 172..177
/sec_str_type="sheet"
/note="strand 1"
SecStr 180..185
/sec_str_type="sheet"
/note="strand 2"
SecStr 186..216
/sec_str_type="helix"
/note="helix 8"
Het join(bond(194),bond(272))
/heterogen="( HG,1003 )"
Het bond(196)
/heterogen="( HG,1005 )"
Het join(bond(196),bond(196))
/heterogen="( HG,1002 )"
Het join(bond(210),bond(214),bond(214))
/heterogen="( HG,1004 )"
SecStr 225..253
/sec_str_type="helix"
/note="helix 9"
SecStr 260..269
/sec_str_type="helix"
/note="helix 10"
Bond bond(268,272)
/bond_type="disulfide"
SecStr 270..285
/sec_str_type="helix"
/note="helix 11"
Het join(bond(284),bond(305),bond(309),bond(305))
/heterogen="( HG,1006 )"
SecStr 301..319
/sec_str_type="helix"
/note="helix 12"
ORIGIN
1 ayttfsatkn dqlkepmffg qpvqvarydq qkydifekli ekqlsffwrp eevdvsrdri
61 dyqalpehek hifisnlkyq tlldsiqgrs pnvallplis ipeletwvet wafsetihsr
121 sythiirniv ndpsvvfddi vtneqiqkra egissyydel iemtsywhll gegthtvngk
181 tvtvslrelk kklylclmsv naleairfyv sfacsfafae relmegnaki irliardeal
241 hltgtqhmln llrsgaddpe maeiaeeckq ecydlfvqaa qqekdwadyl frdgsmigln
301 kdilcqyvey itnirmqavg ldlpfntrsn pipwintwlv sdnvqvapqe vevssylvgq
361 idsevdtddl snfql
//
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