Structure of PDB 8p28 Chain A

Receptor sequence
>8p28A (length=645) Species: 165179 (Segatella copri) [Search protein sequence]
MIQTVVKRDGRIVGFNEQKIMAAIRKAMLHTDKGEDTTLIEQITDHISYR
GKSQMSVEAIQDAIEMELMKSARKDVAQKYIAYRNQRNIARKAKTRDVFM
SDTPAGMMMKFASETTKPFVDDYLLSEDVRDAVMHNYIHIHDKDYYPTKS
LTCVQHPLDVILNHGFTAGHGSSRPAKRIETAAVLACISLETCQNEMHGG
QAIPAFDFYLAPYVRMSYQEEVKNLEKLTGEDLSNLYDAPIDDYIEKPLD
GLQGRERLEQHAINKTVNRVHQAMEAFIHNMNTIHSRVFSSINYGTDTSA
EGRCIMREILQSTYQGVGNGETAIFPIQIWKKKRGVNYLPEDRNYDLYKL
ACKVTARRFFPNFLNLDATFNQNEKWRADDPERYKWEIATMGCRTRVFED
RWGEKTSIARGNLSFSTINIVKLAIECMGIENEKQRIDMFFAKLDNILDI
TAKQLDERFQFQKTAMAKQFPLLMKYLWVGAENLKPEETIESVINHGTLG
IGFIGLAECLVALIGKHHGESEKAQELGLKIITYMRDRANEFSEQYHHNY
SILATPAEGLSGKFTKKDRKQFGVIPGVTDRDYYTNSNHVPVYYKCTALK
KAQIEAPYHDLTRGGHIFYVEINPSVIESVVDMMDKYNMGYGSVN
3D structure
PDB8p28 Activity modulation in anaerobic ribonucleotide reductase: nucleotide binding to the ATP-cone mediates long-range order-disorder transitions in the active site
ChainA
Resolution2.77 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 1.17.4.2: ribonucleoside-triphosphate reductase (thioredoxin).
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 A R192 K195 T199 V202 L203 I206 R174 K177 T181 V184 L185 I188
BS02 DTP A V5 K19 I60 V5 K19 I60
BS03 DTP A R8 A23 K26 H30 Y80 Y83 R87 R91 R8 A23 K26 H30 Y80 Y83 R87 R91
BS04 MG A Q290 E293 Q272 E275
BS05 DTP A A294 H297 A276 H279
Gene Ontology
Molecular Function
GO:0004748 ribonucleoside-diphosphate reductase activity, thioredoxin disulfide as acceptor
GO:0005524 ATP binding
GO:0008998 ribonucleoside-triphosphate reductase (thioredoxin) activity
GO:0016491 oxidoreductase activity
Biological Process
GO:0006260 DNA replication
GO:0009265 2'-deoxyribonucleotide biosynthetic process
Cellular Component
GO:0031250 anaerobic ribonucleoside-triphosphate reductase complex

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Molecular Function

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Biological Process

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Cellular Component
External links
PDB RCSB:8p28, PDBe:8p28, PDBj:8p28
PDBsum8p28
PubMed38968292
UniProtA0A3E4SF67

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