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3GUT

Crystal structure of a higher-order complex of p50:RelA bound to the HIV-1 LTR

Functional Information from GO Data
ChainGOidnamespacecontents
A0003677molecular_functionDNA binding
A0003700molecular_functionDNA-binding transcription factor activity
A0005737cellular_componentcytoplasm
A0006355biological_processregulation of DNA-templated transcription
B0003677molecular_functionDNA binding
B0003700molecular_functionDNA-binding transcription factor activity
B0005737cellular_componentcytoplasm
B0006355biological_processregulation of DNA-templated transcription
C0003677molecular_functionDNA binding
C0003700molecular_functionDNA-binding transcription factor activity
C0005737cellular_componentcytoplasm
C0006355biological_processregulation of DNA-templated transcription
D0003677molecular_functionDNA binding
D0003700molecular_functionDNA-binding transcription factor activity
D0005737cellular_componentcytoplasm
D0006355biological_processregulation of DNA-templated transcription
E0003677molecular_functionDNA binding
E0003700molecular_functionDNA-binding transcription factor activity
E0005737cellular_componentcytoplasm
E0006355biological_processregulation of DNA-templated transcription
F0003677molecular_functionDNA binding
F0003700molecular_functionDNA-binding transcription factor activity
F0005737cellular_componentcytoplasm
F0006355biological_processregulation of DNA-templated transcription
G0003677molecular_functionDNA binding
G0003700molecular_functionDNA-binding transcription factor activity
G0005737cellular_componentcytoplasm
G0006355biological_processregulation of DNA-templated transcription
H0003677molecular_functionDNA binding
H0003700molecular_functionDNA-binding transcription factor activity
H0005737cellular_componentcytoplasm
H0006355biological_processregulation of DNA-templated transcription
Functional Information from PROSITE/UniProt
site_idPS01204
Number of Residues7
DetailsREL_1 NF-kappa-B/Rel/dorsal domain signature. FRYvCEG
ChainResidueDetails
BPHE355-GLY361
APHE34-GLY40

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsMOD_RES: S-nitrosocysteine; alternate => ECO:0000269|PubMed:8710491
ChainResidueDetails
BCYS359
DCYS359
FCYS359
HCYS359

site_idSWS_FT_FI2
Number of Residues4
DetailsMOD_RES: Phosphoserine; by PKA => ECO:0000255
ChainResidueDetails
BSER635
DSER635
FSER635
HSER635

site_idSWS_FT_FI3
Number of Residues4
DetailsLIPID: S-(15-deoxy-Delta12,14-prostaglandin J2-9-yl)cysteine; alternate => ECO:0000269|PubMed:11466314
ChainResidueDetails
BCYS359
DCYS359
FCYS359
HCYS359
ELYS122
ELYS123
GLYS122
GLYS123

site_idSWS_FT_FI4
Number of Residues8
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) => ECO:0007744|PubMed:28112733
ChainResidueDetails
BLYS623
ALYS221
DLYS623
CLYS221
FLYS623
ELYS221
HLYS623
GLYS221

site_idSWS_FT_FI5
Number of Residues4
DetailsMOD_RES: Phosphothreonine => ECO:0000269|PubMed:14690596
ChainResidueDetails
ATHR254
CTHR254
ETHR254
GTHR254

site_idSWS_FT_FI6
Number of Residues4
DetailsMOD_RES: Phosphoserine; by RPS6KA4 and RPS6KA5 => ECO:0000269|PubMed:12628924
ChainResidueDetails
ASER276
CSER276
ESER276
GSER276

site_idSWS_FT_FI7
Number of Residues4
DetailsMOD_RES: Phosphoserine => ECO:0000305|PubMed:15516339
ChainResidueDetails
ASER281
CSER281
ESER281
GSER281

site_idSWS_FT_FI8
Number of Residues4
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO3) => ECO:0000269|PubMed:22649547
ChainResidueDetails
ALYS37
CLYS37
ELYS37
GLYS37

site_idSWS_FT_FI9
Number of Residues12
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO3); alternate
ChainResidueDetails
GLYS122
GLYS123
ALYS122
ALYS123
CLYS122
CLYS123
ELYS122
ELYS123

222624

PDB entries from 2024-07-17

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