Structure of PDB 4ii3 Chain C

Receptor sequence
>4ii3C (length=977) Species: 284812 (Schizosaccharomyces pombe 972h-) [Search protein sequence]
TIDEGLYSRQLYVLGHEAMKQMSQSNVLIIGCKGLGVEIAKNVCLAGVKS
VTLYDPQPTRIEDLSSQYFLTEDDIGVPRAKVTVSKLAELNQYVPVSVVD
ELSTEYLKNFKCVVVTETSLTKQLEINDFTHKNHIAYIAADSRGLFGSIF
CDFGENFICTDTDGNEPLTGMIASITDDGVVTMLEETRHGLENGDFVKFT
EVKGMPGLNDGTPRKVEVKGPYTFSIGSVKDLGSAGYNGVFTQVKVPTKI
SFKSLRESLKDPEYVYPDFGKMMRPPQYHIAFQALSAFADAHEGSLPRPR
NDIDAAEFFEFCKKIASTLQFDVELDEKLIKEISYQARGDLVAMSAFLGG
AVAQEVLKATTSKFYPLKQYFYFDSLESLPSSVTISEETCKPRGCRYDGQ
IAVFGSEFQEKIASLSTFLVGAGAIGCEMLKNWAMMGVATGESGHISVTD
MDSIEKSNLNRQFLFRPRDVGKLKSECASTAVSIMNPSLTGKITSYQERV
GPESEGIFGDEFFEKLSLVTNALDNVEARMYVDRRCVFFEKPLLESGTLG
TKGNTQVVVPHLTESYGSSQDPPEKSFPICTLKNFPNRIEHTIAWARDLF
EGLFKQPIDNVNMYLSSPNFLETSLKTSSNPREVLENIRDYLVTEKPLSF
EECIMWARLQFDKFFNNNIQQLLFNFPKDSVTSTGQPFWSGPKRAPTPLS
FDIHNREHFDFIVAAASLYAFNYGLKSETDPAIYERVLAGYNPPPFAPKS
GIAANKDKQELKSIADSLRLTPAEFEKDDDSNHHIDFITAASNLRAMNYD
ITPADRFKTKFVAGKIVPAMCTSTAVVSGLVCLELVKLVDGKKKIEEYKN
GFFNLAIGLFTFSDPIASPKMKVNGKEIDKIWDRYNLPDCTLQELIDYFQ
KEEGLEVTMLSSGVSLLYANFQPPKKLAERLPLKISELVEQITKKKLEPF
RKHLVLEICCDDANGEDVEVPFICIKL
3D structure
PDB4ii3 Structure of a ubiquitin E1-E2 complex: insights to E1-E2 thioester transfer.
ChainC
Resolution2.9 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 ATP C R22 A437 D463 M464 R474 K487 R512 V513 A535 L536 D537 N538 R9 A424 D450 M451 R461 K474 R499 V500 A522 L523 D524 N525
BS02 CA C D611 Q619 D598 Q606
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:4ii3, PDBe:4ii3, PDBj:4ii3
PDBsum4ii3
PubMed23416107
UniProtO94609|UBA1_SCHPO Ubiquitin-activating enzyme E1 1 (Gene Name=ptr3)

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