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4LJP

Structure of an active ligase (HOIP-H889A)/ubiquitin transfer complex

Functional Information from GO Data
ChainGOidnamespacecontents
A0004842molecular_functionubiquitin-protein transferase activity
A0008270molecular_functionzinc ion binding
A0071797cellular_componentLUBAC complex
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 1101
ChainResidue
ACYS871
ACYS874
ACYS890
ACYS893

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 1102
ChainResidue
ACYS898
ACYS901
AHIS926
ACYS930

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 1103
ChainResidue
ACYS916
AHIS923
AHIS925
ACYS911

site_idAC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 1104
ChainResidue
ACYS969
ACYS986
ACYS998
AHIS1001

Functional Information from PROSITE/UniProt
site_idPS00299
Number of Residues26
DetailsUBIQUITIN_1 Ubiquitin domain signature. KakIqDkegIPpdqQrLIFaGkqleD
ChainResidueDetails
BLYS27-ASP52

site_idPS00518
Number of Residues10
DetailsZF_RING_1 Zinc finger RING-type signature. CrHqFCsgCY
ChainResidueDetails
ACYS893-TYR902

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues30
DetailsZinc finger: {"description":"RING-type 2; atypical","evidences":[{"source":"PROSITE-ProRule","id":"PRU01221","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues1
DetailsActive site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU01221","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues8
DetailsBinding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU01221","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues2
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

site_idSWS_FT_FI5
Number of Residues75
DetailsDomain: {"description":"Ubiquitin-like","evidences":[{"source":"PROSITE-ProRule","id":"PRU00214","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues2
DetailsSite: {"description":"Interacts with activating enzyme"}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues1
DetailsSite: {"description":"Essential for function"}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine; by PINK1","evidences":[{"source":"UniProtKB","id":"P62987","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI9
Number of Residues1
DetailsModified residue: {"description":"ADP-ribosylglycine","evidences":[{"source":"UniProtKB","id":"P62987","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI10
Number of Residues7
DetailsCross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)","evidences":[{"source":"UniProtKB","id":"P62987","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI11
Number of Residues2
DetailsCross-link: {"description":"Glycyl lysine isopeptide (Gly-Lys) (interchain with K-? in acceptor proteins)"}
ChainResidueDetails

239492

PDB entries from 2025-07-30

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