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4LJQ

Crystal structure of the catalytic core of E3 ligase HOIP

Functional Information from GO Data
ChainGOidnamespacecontents
A0004842molecular_functionubiquitin-protein transferase activity
A0008270molecular_functionzinc ion binding
A0071797cellular_componentLUBAC complex
B0004842molecular_functionubiquitin-protein transferase activity
B0008270molecular_functionzinc ion binding
B0071797cellular_componentLUBAC complex
C0004842molecular_functionubiquitin-protein transferase activity
C0008270molecular_functionzinc ion binding
C0071797cellular_componentLUBAC complex
D0004842molecular_functionubiquitin-protein transferase activity
D0008270molecular_functionzinc ion binding
D0071797cellular_componentLUBAC complex
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN B 1101
ChainResidue
BCYS871
BCYS874
BCYS890
BCYS893

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN B 1102
ChainResidue
BCYS898
BCYS901
BHIS926
BCYS930

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN B 1103
ChainResidue
BCYS916
BHIS923
BHIS925
BCYS911

site_idAC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN B 1104
ChainResidue
BCYS969
BCYS986
BCYS998
BHIS1001

site_idAC5
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN B 1105
ChainResidue
BHIS887
BHIS889
CHIS887
CHIS889

site_idAC6
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 1101
ChainResidue
ACYS871
ACYS874
ACYS890
ACYS893

site_idAC7
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 1102
ChainResidue
ACYS898
ACYS901
AHIS926
ACYS930

site_idAC8
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 1103
ChainResidue
ACYS911
ACYS916
AHIS923
AHIS925

site_idAC9
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 1104
ChainResidue
ACYS969
ACYS986
ACYS998
AHIS1001

site_idBC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 1105
ChainResidue
AHIS887
AHIS889
DHIS887
DHIS889

site_idBC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN C 1101
ChainResidue
CCYS871
CCYS874
CCYS890
CCYS893

site_idBC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN C 1102
ChainResidue
CCYS898
CCYS901
CHIS926
CCYS930

site_idBC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN C 1103
ChainResidue
CCYS911
CCYS916
CHIS923
CHIS925

site_idBC5
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN C 1104
ChainResidue
CCYS969
CCYS986
CCYS998
CHIS1001

site_idBC6
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN D 1101
ChainResidue
DCYS871
DCYS874
DCYS890
DCYS893

site_idBC7
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN D 1102
ChainResidue
DCYS898
DCYS901
DHIS926
DCYS930

site_idBC8
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN D 1103
ChainResidue
DCYS911
DCYS916
DHIS923
DHIS925

site_idBC9
Number of Residues5
DetailsBINDING SITE FOR RESIDUE ZN D 1104
ChainResidue
DCYS969
DVAL971
DCYS986
DCYS998
DHIS1001

Functional Information from PROSITE/UniProt
site_idPS00518
Number of Residues10
DetailsZF_RING_1 Zinc finger RING-type signature. CrHqFCsgCY
ChainResidueDetails
BCYS893-TYR902

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsActive site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU01221","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues32
DetailsBinding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU01221","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues8
DetailsCross-link: {"description":"(Microbial infection) Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)","evidences":[{"source":"PubMed","id":"27572974","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

242199

PDB entries from 2025-09-24

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