Structure of PDB 5olk Chain B

Receptor sequence
>5olkB (length=392) Species: 398720 (Leeuwenhoekiella blandensis MED217) [Search protein sequence]
KKIIKRDYSTAPFVLEKITNAIANAMAALGHGSEQDAKLISMQVYESLLN
NKEQESEYIPTVEQVQDMVEDKLMSSEFHDVAKAYIIYRNKRALERKTNI
FEKRINLKPYEYPELNEYVAAIRHSYWIHTEFNFTSDIQDFKTGLSEVER
SAIKNTMLAISQIEVAVKTFWGDVHHRLPKPEIAAVGATFAESEVRHHDA
YSHLLEILGLNEEFKELKKKPVIMKRVHYLETSLKHAKSDDDREYTESIL
LFALFIEHVSLFSQFLIIMAFNKHKNMLKGISNAVEATSKEEQIHGDFGV
DIINIIKKENPEWFDEEHNNLIKEMCLNSFEAESKVVDWIFEKGELDFLP
KAVINEFLKNRFNKSLEAIGLEKLFDIDEALLQETEWFDDEI
3D structure
PDB5olk Novel ATP-cone-driven allosteric regulation of ribonucleotide reductase via the radical-generating subunit.
ChainB
Resolution2.45 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 1.17.4.1: ribonucleoside-diphosphate reductase.
Interaction with ligand
Site
#		 Ligand Ligand
chain		 Binding residues on receptor
(original residue number in PDB)		 Binding residues on receptor
(residue number reindexed from 1)		 Binding affinity
BS01 DTP B I9 K11 R12 F19 V20 K23 I24 V68 V71 Q72 I3 K5 R6 F13 V14 K17 I18 V62 V65 Q66 MOAD: Kd=1uM
BS02 DTP B R12 A27 A31 A34 A90 Y91 Y94 R98 R102 R6 A21 A25 A28 A84 Y85 Y88 R92 R96 MOAD: Kd=1uM
BS03 MN B E170 E200 H203 E298 E164 E194 H197 E292
BS04 MN B E200 E263 E298 H301 E194 E257 E292 H295
Gene Ontology
Molecular Function
GO:0004748 ribonucleoside-diphosphate reductase activity, thioredoxin disulfide as acceptor
GO:0005524 ATP binding
GO:0016491 oxidoreductase activity
GO:0046872 metal ion binding
Biological Process
GO:0009263 deoxyribonucleotide biosynthetic process

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Molecular Function
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Biological Process
External links
PDB RCSB:5olk, PDBe:5olk, PDBj:5olk
PDBsum5olk
PubMed29388911
UniProtA3XHF9

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