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6SC6

dAb3/HOIP-RBR apo structure

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
ACYS699
ACYS702
ACYS722
ACYS725

site_idAC2
Number of Residues4
Detailsbinding site for residue ZN A 1102
ChainResidue
ACYS717
ACYS719
ACYS744
ACYS747

site_idAC3
Number of Residues4
Detailsbinding site for residue ZN A 1103
ChainResidue
ACYS802
ACYS817
ACYS820
ACYS799

site_idAC4
Number of Residues4
Detailsbinding site for residue ZN A 1104
ChainResidue
ACYS825
ACYS828
AHIS836
ACYS841

site_idAC5
Number of Residues4
Detailsbinding site for residue ZN A 1105
ChainResidue
ACYS871
ACYS874
ACYS890
ACYS893

site_idAC6
Number of Residues4
Detailsbinding site for residue ZN A 1106
ChainResidue
ACYS898
ACYS901
AHIS926
ACYS930

site_idAC7
Number of Residues4
Detailsbinding site for residue ZN A 1107
ChainResidue
ACYS911
ACYS916
AHIS923
AHIS925

site_idAC8
Number of Residues4
Detailsbinding site for residue ZN A 1108
ChainResidue
ACYS969
ACYS986
ACYS998
AHIS1001

site_idAC9
Number of Residues9
Detailsbinding site for residue SO4 A 1109
ChainResidue
AASN903
APRO927
AGLY1064
AGLN1065
AHOH1203
AHOH1213
AHOH1227
AHOH1228
AHOH1239

site_idAD1
Number of Residues5
Detailsbinding site for residue SO4 A 1110
ChainResidue
AGLY884
ACYS885
AMET886
APHE932
AARG935

site_idAD2
Number of Residues1
Detailsbinding site for residue SO4 A 1111
ChainResidue
AARG1032

site_idAD3
Number of Residues3
Detailsbinding site for residue CL A 1112
ChainResidue
ATRP798
ALYS829
BGLY104

site_idAD4
Number of Residues4
Detailsbinding site for residue CL A 1113
ChainResidue
AGLY900
ACYS930
ALEU931
AASN1011

site_idAD5
Number of Residues5
Detailsbinding site for residue SO4 B 201
ChainResidue
AHOH1223
BSER52
BPRO53
BILE54
BTHR56

site_idAD6
Number of Residues3
Detailsbinding site for residue SO4 B 202
ChainResidue
BPHE27
BTHR28
BTYR32

Functional Information from PROSITE/UniProt
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 Residues50
DetailsZN_FING: RING-type 1 => ECO:0000255|PROSITE-ProRule:PRU01221
ChainResidueDetails
ACYS699-ARG749

site_idSWS_FT_FI2
Number of Residues62
DetailsZN_FING: IBR-type => ECO:0000255|PROSITE-ProRule:PRU01221
ChainResidueDetails
AALA779-CYS841

site_idSWS_FT_FI3
Number of Residues30
DetailsZN_FING: RING-type 2; atypical => ECO:0000255|PROSITE-ProRule:PRU01221
ChainResidueDetails
ACYS871-CYS901

site_idSWS_FT_FI4
Number of Residues1
DetailsACT_SITE: ACT_SITE => ECO:0000255|PROSITE-ProRule:PRU01221
ChainResidueDetails
ACYS885

site_idSWS_FT_FI5
Number of Residues4
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU01221, ECO:0000269|PubMed:35294289, ECO:0007744|PDB:7V8F, ECO:0007744|PDB:7V8G
ChainResidueDetails
ACYS699
ACYS702
ACYS722
ACYS725

site_idSWS_FT_FI6
Number of Residues4
DetailsBINDING: BINDING => ECO:0000269|PubMed:35294289, ECO:0007744|PDB:7V8F, ECO:0007744|PDB:7V8G
ChainResidueDetails
ACYS717
ACYS719
ACYS744
ACYS747

site_idSWS_FT_FI7
Number of Residues16
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU01221
ChainResidueDetails
ACYS799
ACYS874
ACYS890
ACYS893
ACYS898
ACYS901
ACYS916
AHIS925
ACYS802
ACYS817
ACYS820
ACYS825
ACYS828
AHIS836
ACYS841
ACYS871

site_idSWS_FT_FI8
Number of Residues4
DetailsCROSSLNK: (Microbial infection) Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:27572974
ChainResidueDetails
ALYS735
ALYS783
ALYS875

218853

PDB entries from 2024-04-24

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