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5AEK

Crystal structure of the human SENP2 C548S in complex with the human SUMO1 K48M F66W

Functional Information from GO Data
ChainGOidnamespacecontents
A0006508biological_processproteolysis
A0008234molecular_functioncysteine-type peptidase activity
C0006508biological_processproteolysis
C0008234molecular_functioncysteine-type peptidase activity
E0006508biological_processproteolysis
E0008234molecular_functioncysteine-type peptidase activity
G0006508biological_processproteolysis
G0008234molecular_functioncysteine-type peptidase activity
I0006508biological_processproteolysis
I0008234molecular_functioncysteine-type peptidase activity
K0006508biological_processproteolysis
K0008234molecular_functioncysteine-type peptidase activity
M0006508biological_processproteolysis
M0008234molecular_functioncysteine-type peptidase activity
O0006508biological_processproteolysis
O0008234molecular_functioncysteine-type peptidase activity
Q0006508biological_processproteolysis
Q0008234molecular_functioncysteine-type peptidase activity
S0006508biological_processproteolysis
S0008234molecular_functioncysteine-type peptidase activity
U0006508biological_processproteolysis
U0008234molecular_functioncysteine-type peptidase activity
W0006508biological_processproteolysis
W0008234molecular_functioncysteine-type peptidase activity
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1968
DetailsRegion: {"description":"Protease","evidences":[{"source":"PubMed","id":"15296745","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues24
DetailsActive site: {"evidences":[{"source":"PubMed","id":"15296745","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues12
DetailsActive site: {"description":"Nucleophile","evidences":[{"source":"PubMed","id":"15296745","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues770
DetailsDomain: {"description":"Ubiquitin-like","evidences":[{"source":"PROSITE-ProRule","id":"PRU00214","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues36
DetailsRegion: {"description":"(Microbial infection) Interaction with Tula hantavirus","evidences":[{"source":"PubMed","id":"12606074","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues12
DetailsSite: {"description":"Interaction with PIAS2"}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues12
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues48
DetailsCross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)","evidences":[{"source":"PubMed","id":"28112733","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI9
Number of Residues24
DetailsCross-link: {"description":"Glycyl lysine isopeptide (Gly-Lys) (interchain with K-? in acceptor proteins)","evidences":[{"source":"PubMed","id":"27068747","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI10
Number of Residues12
DetailsCross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1)"}
ChainResidueDetails

site_idSWS_FT_FI11
Number of Residues12
DetailsCross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)","evidences":[{"source":"PubMed","id":"25755297","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"28112733","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

246704

PDB entries from 2025-12-24

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