Structure of PDB 7k5j Chain K

Receptor sequence
>7k5jK (length=979) Species: 559292 (Saccharomyces cerevisiae S288C) [Search protein sequence]
GEIDESLYSRQLYVLGKEAMLKMQTSNVLILGLKGLGVEIAKNVVLAGVK
SMTVFDPEPVQLADLSTQFFLTEKDIGQKRGDVTRAKLAELNAYVPVNVL
DSLDDVTQLSQFQVVVATDTVSLEDKVKINEFCHSSGIRFISSETRGLFG
NTFVDLGDEFTVLDPTGEEPRTGMVSDIEPDGTVTMLDDNRHGLEDGNFV
RFSEVEGLDKLNDGTLFKVEVLGPFAFRIGSVKEYGEYKKGGIFTEVKVP
RKISFKSLKQQLSNPEFVFSDFAKFDRAAQLHLGFQALHQFAVRHNGELP
RTMNDEDANELIKLVTDLSVQQPEVLGEGVDVNEDLIKELSYQARGDIPG
VVAFFGGLVAQEVLKACSGKFTPLKQFMYFDSLESLPDPKNFPRNEKTTQ
PVNSRYDNQIAVFGLDFQKKIANSKVFLVGSGAIGCEMLKNWALLGLGSG
SDGYIVVTDNDSIEKSNLNRQFLFRPKDVGKNKSEVAAEAVCAMNPDLKG
KINAKIDKVGPETEEIFNDSFWESLDFVTNALDNVDARTYVDRRCVFYRK
PLLESGTLGTKGNTQVIIPRLTESYSSSPLCTLRSFPNKIDHTIAWAKSL
FQGYFTDSAENVNMYLTQPNFVEQTLKDVKGVLESISDSLSSKPHNFEDC
IKWARLEFEKKFNHDIKQLLFNFPKDAKTSNGEPFWSGAKRAPTPLEFDI
YNNDHFHFVVAGASLRAYNYGIKSDDSNSKPNVDEYKSVIDHMIIPEFTP
NEIDQLVSSLPDPSTLAGFKLEPVDFEKDDDTNHHIEFITACSNCRAQNY
FIETADRQKTKFIAGRIIPAIATTTSLVTGLVNLELYKLIDNKTDIEQYK
NGFVNLALPFFGFSEPIASPKGEYNNKKYDKIWDRFDIKGDIKLSDLIEH
FEKDEGLEITMLSYGVSLLYASFFPPKKLKERLNLPITQLVKLVTKKDIP
AHVSTMILEICADDKEGEDVEVPFITIHL
3D structure
PDB7k5j Crystal structures of an E1-E2-ubiquitin thioester mimetic reveal molecular mechanisms of transthioesterification.
ChainK
Resolution3.42 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) R21 R481 D544 C600 T601 R603
Catalytic site (residue number reindexed from 1) R10 R470 D533 C581 T582 R584
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 AMP K D470 K494 K519 V520 L543 D544 D459 K483 K508 V509 L532 D533
Gene Ontology
Molecular Function
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
Biological Process
GO:0006511 ubiquitin-dependent protein catabolic process
GO:0006974 DNA damage response
GO:0016567 protein ubiquitination
GO:0036211 protein modification process
GO:0043412 macromolecule modification
Cellular Component
GO:0005634 nucleus
GO:0005737 cytoplasm

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Molecular Function

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Biological Process

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Cellular Component
External links
PDB RCSB:7k5j, PDBe:7k5j, PDBj:7k5j
PDBsum7k5j
PubMed33888705
UniProtP22515|UBA1_YEAST Ubiquitin-activating enzyme E1 1 (Gene Name=UBA1)

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