Structure of PDB 6o82 Chain C

Receptor sequence
>6o82C (length=975) Species: 284812 (Schizosaccharomyces pombe 972h-) [Search protein sequence]
TIDEGLYSRQLYVLGHEAMKQMSQSNVLIIGCKGLGVEIAKNVCLAGVKS
VTLYDPQPTRIEDLSSQYFLTEDDIGVPRAKVTVSKLAELNQYVPVSVVD
ELSTEYLKNFKCVVVTETSLTKQLEINDFTHKNHIAYIAADSRGLFGSIF
CDFGENFICTDTDGNEPLTGMIASITDDGVVTMLEETRHGLENGDFVKFT
EVKGMPGLNDGTPRKVEVKGPYTFSIGSVKDLGSAGYNGVFTQVKVPTKI
SFKSLRESLKDPEYVYPDFGKMMRPPQYHIAFQALSAFADAHEGSLPRPR
NDIDAAEFFEFCKKIASTLQFDVELDEKLIKEISYQARGDLVAMSAFLGG
AVAQEVLKATTSKFYPLKQYFYFDSLESLPSSVTISEETCKPRGCRYDGQ
IAVFGSEFQEKIASLSTFLVGAGAIGCEMLKNWAMMGVATGESGHISVTD
MDSIEKSNLNRQFLFRPRDVGKLKSECASTAVSIMNPSLTGKITSYQERV
GPESEGIFGDEFFEKLSLVTNALDNVEARMYVDRRCVFFEKPLLESGTLG
TKGNTQVVVPHLTESYGSSQDPPEKSFPICTLKNFPNRIEHTIAWARDLF
EGLFKQPIDNVNMYLSSPNFLETSLKTSSNPREVLENIRDYLVTEKPLSF
EECIMWARLQFDKFFNNNIQQLLFNFPKDSVTSTGQPFWSGPKRAPTPLS
FDIHNREHFDFIVAAASLYAFNYGLKSETDPAIYERVLAGYNPPPFAPKS
AANKDKQELKSIADSLRLTPAEFEKDDDSNHHIDFITAASNLRAMNYDIT
PADRFKTKFVAGKIVPAMCTSTAVVSGLVCLELVKLVDGKKKIEEYKNGF
FNLAIGLFTFSDPIASPKMKVNGKEIDKIWDRYNLPDCTLQELIDYFQKE
EGLEVTMLSSGVSLLYANFQPPKKLAERLPLKISELVEQITKKKLEPFRK
HLVLEICCDDANGEDVEVPFICIKL
3D structure
PDB6o82 Structural basis for adenylation and thioester bond formation in the ubiquitin E1.
ChainC
Resolution2.604 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) R22 R474 D537 C593 T594 K596
Catalytic site (residue number reindexed from 1) R9 R461 D524 C580 T581 K583
Enzyme Commision number 6.2.1.45: E1 ubiquitin-activating enzyme.
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 MG C D465 E468 D452 E455
BS02 POP C R22 N471 R474 K487 R9 N458 R461 K474
BS03 JZU C A437 D463 M464 R474 K487 R512 V513 A535 L536 D537 N538 A424 D450 M451 R461 K474 R499 V500 A522 L523 D524 N525
Gene Ontology
Molecular Function
GO:0000287 magnesium ion binding
GO:0004839 ubiquitin activating enzyme activity
GO:0005515 protein binding
GO:0005524 ATP binding
GO:0008641 ubiquitin-like modifier activating enzyme activity
GO:0016874 ligase activity
GO:0016887 ATP hydrolysis activity
Biological Process
GO:0006511 ubiquitin-dependent protein catabolic process
GO:0006974 DNA damage response
GO:0016567 protein ubiquitination
GO:0036211 protein modification process
Cellular Component
GO:0005634 nucleus
GO:0005737 cytoplasm
GO:0005829 cytosol

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Molecular Function

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Biological Process

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Cellular Component
External links
PDB RCSB:6o82, PDBe:6o82, PDBj:6o82
PDBsum6o82
PubMed31235585
UniProtO94609|UBA1_SCHPO Ubiquitin-activating enzyme E1 1 (Gene Name=ptr3)

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