Structure of PDB 5olk Chain D

Receptor sequence
>5olkD (length=393) Species: 398720 (Leeuwenhoekiella blandensis MED217) [Search protein sequence]
IKKIIKRDYSTAPFVLEKITNAIANAMAALGHGSEQDAKLISMQVYESLL
NNKEQESEYIPTVEQVQDMVEDKLMSSEFHDVAKAYIIYRNKRALERKTN
IFEKRINLKPYEYPELNEYVAAIRHSYWIHTEFNFTSDIQDFKTGLSEVE
RSAIKNTMLAISQIEVAVKTFWGDVHHRLPKPEIAAVGATFAESEVRHHD
AYSHLLEILGLNEEFKELKKKPVIMKRVHYLETSLKHAKSDDDREYTESI
LLFALFIEHVSLFSQFLIIMAFNKHKNMLKGISNAVEATSKEEQIHGDFG
VDIINIIKKENPEWFDEEHNNLIKEMCLNSFEAESKVVDWIFEKGELDFL
PKAVINEFLKNRFNKSLEAIGLEKLFDIDEALLQETEWFDDEI
3D structure
PDB5olk Novel ATP-cone-driven allosteric regulation of ribonucleotide reductase via the radical-generating subunit.
ChainD
Resolution2.45 Å
3D
structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
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 D I9 K11 R12 F19 V20 K23 I24 V68 V71 Q72 I4 K6 R7 F14 V15 K18 I19 V63 V66 Q67 MOAD: Kd=1uM
BS02 DTP D R12 A27 N30 A31 Y91 Y94 R98 R102 R7 A22 N25 A26 Y86 Y89 R93 R97 MOAD: Kd=1uM
BS03 MN D E170 E200 H203 E298 E165 E195 H198 E293
BS04 MN D E200 E263 E298 H301 E195 E258 E293 H296
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

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

[Back to BioLiP]