Structure of PDB 8p2c Chain D

Receptor sequence
>8p2cD (length=647) Species: 165179 (Segatella copri) [Search protein sequence]
MIQTVVKRDGRIVGFNEQKIMAAIRKAMLHTDKGEDTTLIEQITDHISYR
GKSQMSVEAIQDAIEMELMKSARKDVAQKYIAYRNQRNIARKAKTRDVFM
SIVDTPAGMMMKFASETTKPFVDDYLLSEDVRDAVMHNYIHIHDKDYYPT
KSLTCVQHPLDVILNHGFTAGHGSSRPAKRIETAAVLACISLETCQNEMH
GGQAIPAFDFYLAPYVRMSYQEEVKNLEKLTGEDLSNLYDAPIDDYIEKP
LDGLQGRERLEQHAINKTVNRVHQAMEAFIHNMNTIHSRVFSSINYGTDT
SAEGRCIMREILQSTYQGVGNGETAIFPIQIWKKKRGVNYLPEDRNYDLY
KLACKVTARRFFPNFLNLDATFNQNEKWRADDPERYKWEIATMGCRTRVF
EDRWGEKTSIARGNLSFSTINIVKLAIECMGIENEKQRIDMFFAKLDNIL
DITAKQLDERFQFQKTAMAKQFPLLMKYLWVGAENLKPEETIESVINHGT
LGIGFIGLAECLVALIGKHHGESEKAQELGLKIITYMRDRANEFSEQYHH
NYSILATPAEGLSGKFTKKDRKQFGVIPGVTDRDYYTNSNHVPVYYKCTA
LKKAQIEAPYHDLTRGGHIFYVEINPSVIESVVDMMDKYNMGYGSVN
3D structure
PDB8p2c Activity modulation in anaerobic ribonucleotide reductase: nucleotide binding to the ATP-cone mediates long-range order-disorder transitions in the active site
ChainD
Resolution2.59 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 D Q290 H297 Q274 H281
BS02 DTP D R192 R196 T199 V202 R176 R180 T183 V186
BS03 DTP D R8 N16 K19 I20 R8 N16 K19 I20
BS04 DTP D H30 Y80 Y83 R87 R91 H30 Y80 Y83 R87 R91
BS05 MG D Q290 E293 Q274 E277
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:8p2c, PDBe:8p2c, PDBj:8p2c
PDBsum8p2c
PubMed38968292
UniProtA0A3E4SF67

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