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7ZH9

Uba1 in complex with ATP

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0004839molecular_functionubiquitin activating enzyme activity
A0005515molecular_functionprotein binding
A0005524molecular_functionATP binding
A0005634cellular_componentnucleus
A0005737cellular_componentcytoplasm
A0006511biological_processubiquitin-dependent protein catabolic process
A0006974biological_processDNA damage response
A0008641molecular_functionubiquitin-like modifier activating enzyme activity
A0016567biological_processprotein ubiquitination
A0016874molecular_functionligase activity
A0036211biological_processprotein modification process
A0046872molecular_functionmetal ion binding
Functional Information from PROSITE/UniProt
site_idPS00536
Number of Residues9
DetailsUBIQUITIN_ACTIVAT_1 Ubiquitin-activating enzyme signature 1. KACSGKFtP
ChainResidueDetails
ALYS376-PRO384

site_idPS00865
Number of Residues9
DetailsUBIQUITIN_ACTIVAT_2 Ubiquitin-activating enzyme active site. PLCTLRsFP
ChainResidueDetails
APRO598-PRO606

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues137
DetailsRepeat: {"description":"1-1"}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues154
DetailsRepeat: {"description":"1-2"}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues552
DetailsRegion: {"description":"2 approximate repeats"}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues1
DetailsActive site: {"description":"Glycyl thioester intermediate","evidences":[{"source":"PROSITE-ProRule","id":"PRU10132","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"24816100","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues7
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"35970836","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"7ZH9","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues5
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"35970836","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"24816100","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"7ZH9","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"17287358","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"18407956","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI9
Number of Residues3
DetailsCross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)","evidences":[{"source":"PubMed","id":"22106047","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idMCSA1
Number of Residues8
DetailsM-CSA 307
ChainResidueDetails
AARG21electrostatic stabiliser, hydrogen bond donor, steric role
AARG481electrostatic stabiliser, hydrogen bond donor, steric role
AASP544steric role
ACYS600activator, covalently attached, hydrogen bond donor, nucleophile, proton donor
ATHR601hydrogen bond acceptor, hydrogen bond donor, increase acidity, increase nucleophilicity, proton acceptor, proton donor, proton relay
AARG603electrostatic stabiliser, hydrogen bond donor
AASN781electrostatic stabiliser, hydrogen bond donor
AASP782electrostatic stabiliser, hydrogen bond donor

site_idMCSA2
Number of Residues5
DetailsM-CSA 939
ChainResidueDetails
ACYS600nucleofuge
ATHR601modifies pKa
AARG603electrostatic stabiliser
AASN781electrostatic stabiliser
AASP782electrostatic stabiliser

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PDB entries from 2026-01-28

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