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5DKA

A C2HC zinc finger is essential for the activity of the RING ubiquitin ligase RNF125

Functional Information from GO Data
ChainGOidnamespacecontents
A0000139cellular_componentGolgi membrane
A0000209biological_processprotein polyubiquitination
A0002039molecular_functionp53 binding
A0002250biological_processadaptive immune response
A0005515molecular_functionprotein binding
A0005794cellular_componentGolgi apparatus
A0006511biological_processubiquitin-dependent protein catabolic process
A0008270molecular_functionzinc ion binding
A0016020cellular_componentmembrane
A0016567biological_processprotein ubiquitination
A0016740molecular_functiontransferase activity
A0031624molecular_functionubiquitin conjugating enzyme binding
A0032480biological_processnegative regulation of type I interferon production
A0034098cellular_componentVCP-NPL4-UFD1 AAA ATPase complex
A0039536biological_processnegative regulation of RIG-I signaling pathway
A0043231cellular_componentintracellular membrane-bounded organelle
A0046872molecular_functionmetal ion binding
A0061630molecular_functionubiquitin protein ligase activity
A1990830biological_processcellular response to leukemia inhibitory factor
B0000139cellular_componentGolgi membrane
B0000209biological_processprotein polyubiquitination
B0002039molecular_functionp53 binding
B0002250biological_processadaptive immune response
B0005515molecular_functionprotein binding
B0005794cellular_componentGolgi apparatus
B0006511biological_processubiquitin-dependent protein catabolic process
B0008270molecular_functionzinc ion binding
B0016020cellular_componentmembrane
B0016567biological_processprotein ubiquitination
B0016740molecular_functiontransferase activity
B0031624molecular_functionubiquitin conjugating enzyme binding
B0032480biological_processnegative regulation of type I interferon production
B0034098cellular_componentVCP-NPL4-UFD1 AAA ATPase complex
B0039536biological_processnegative regulation of RIG-I signaling pathway
B0043231cellular_componentintracellular membrane-bounded organelle
B0046872molecular_functionmetal ion binding
B0061630molecular_functionubiquitin protein ligase activity
B1990830biological_processcellular response to leukemia inhibitory factor
Functional Information from PDB Data
site_idAC1
Number of Residues4
Detailsbinding site for residue ZN A 301
ChainResidue
ACYS37
ACYS40
ACYS57
ACYS60

site_idAC2
Number of Residues4
Detailsbinding site for residue ZN A 302
ChainResidue
ACYS100
ACYS103
AHIS115
ACYS119

site_idAC3
Number of Residues4
Detailsbinding site for residue ZN A 303
ChainResidue
AHIS54
ACYS72
ACYS75
ACYS52

site_idAC4
Number of Residues2
Detailsbinding site for residue CL A 304
ChainResidue
ATHR105
ALEU106

site_idAC5
Number of Residues4
Detailsbinding site for residue ZN B 301
ChainResidue
BCYS37
BCYS40
BCYS57
BCYS60

site_idAC6
Number of Residues4
Detailsbinding site for residue ZN B 302
ChainResidue
BCYS100
BCYS103
BHIS115
BCYS119

site_idAC7
Number of Residues4
Detailsbinding site for residue ZN B 303
ChainResidue
BCYS52
BHIS54
BCYS72
BCYS75

site_idAC8
Number of Residues3
Detailsbinding site for residue MG B 304
ChainResidue
BASP36
BVAL43
BLYS98

site_idAC9
Number of Residues1
Detailsbinding site for residue CL B 305
ChainResidue
BTRP70

site_idAD1
Number of Residues3
Detailsbinding site for residue CL B 306
ChainResidue
AHOH408
BALA77
BTYR78

site_idAD2
Number of Residues1
Detailsbinding site for residue CL B 307
ChainResidue
BLEU106

Functional Information from PROSITE/UniProt
site_idPS00518
Number of Residues10
DetailsZF_RING_1 Zinc finger RING-type signature. CgHvFCrsCI
ChainResidueDetails
ACYS52-ILE61

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues78
DetailsZN_FING: RING-type => ECO:0000255|PROSITE-ProRule:PRU00175
ChainResidueDetails
ACYS37-ARG76
BCYS37-ARG76

site_idSWS_FT_FI2
Number of Residues38
DetailsZN_FING: C2HC RNF-type => ECO:0000255|PROSITE-ProRule:PRU01144, ECO:0000303|PubMed:17990982
ChainResidueDetails
ACYS100-CYS119
BCYS100-CYS119

site_idSWS_FT_FI3
Number of Residues16
DetailsBINDING: BINDING => ECO:0000269|PubMed:27411375, ECO:0007744|PDB:5DKA
ChainResidueDetails
ACYS37
BCYS40
BCYS52
BHIS54
BCYS57
BCYS60
BCYS72
BCYS75
ACYS40
ACYS52
AHIS54
ACYS57
ACYS60
ACYS72
ACYS75
BCYS37

site_idSWS_FT_FI4
Number of Residues8
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU01144, ECO:0000269|PubMed:27411375, ECO:0007744|PDB:5DKA
ChainResidueDetails
ACYS100
ACYS103
AHIS115
ACYS119
BCYS100
BCYS103
BHIS115
BCYS119

site_idSWS_FT_FI5
Number of Residues2
DetailsLIPID: N-myristoyl glycine => ECO:0000269|PubMed:17990982
ChainResidueDetails
AGLY2
BGLY2

223166

PDB entries from 2024-07-31

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