Structure of PDB 5olk Chain C

Receptor sequence
>5olkC (length=394) Species: 398720 (Leeuwenhoekiella blandensis MED217) [Search protein sequence]
EIKKIIKRDYSTAPFVLEKITNAIANAMAALGHGSEQDAKLISMQVYESL
LNNKEQESEYIPTVEQVQDMVEDKLMSSEFHDVAKAYIIYRNKRALERKT
NIFEKRINLKPYEYPELNEYVAAIRHSYWIHTEFNFTSDIQDFKTGLSEV
ERSAIKNTMLAISQIEVAVKTFWGDVHHRLPKPEIAAVGATFAESEVRHH
DAYSHLLEILGLNEEFKELKKKPVIMKRVHYLETSLKHAKSDDDREYTES
ILLFALFIEHVSLFSQFLIIMAFNKHKNMLKGISNAVEATSKEEQIHGDF
GVDIINIIKKENPEWFDEEHNNLIKEMCLNSFEAESKVVDWIFEKGELDF
LPKAVINEFLKNRFNKSLEAIGLEKLFDIDEALLQETEWFDDEI
3D structure
PDB5olk Novel ATP-cone-driven allosteric regulation of ribonucleotide reductase via the radical-generating subunit.
ChainC
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 C I9 K11 R12 F19 V20 K23 I24 V68 V71 Q72 I5 K7 R8 F15 V16 K19 I20 V64 V67 Q68 MOAD: Kd=1uM
BS02 DTP C R12 A27 N30 A31 A90 Y91 Y94 R98 R102 R8 A23 N26 A27 A86 Y87 Y90 R94 R98 MOAD: Kd=1uM
BS03 MN C E170 E200 H203 E298 E166 E196 H199 E294
BS04 MN C E200 E263 E298 H301 E196 E259 E294 H297
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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