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SummaryStructural detailsExperimental detailsFunctional detailsSequence NeighborHistoryDownloads

6GHD

Structural analysis of the ternary complex between lamin A/C, BAF and emerin identifies an interface disrupted in autosomal recessive progeroid diseases

Functional Information from GO Data
ChainGOidnamespacecontents
A0000785cellular_componentchromatin
A0000793cellular_componentcondensed chromosome
A0003677molecular_functionDNA binding
A0003690molecular_functiondouble-stranded DNA binding
A0005515molecular_functionprotein binding
A0005634cellular_componentnucleus
A0005635cellular_componentnuclear envelope
A0005654cellular_componentnucleoplasm
A0005694cellular_componentchromosome
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0006325biological_processchromatin organization
A0006979biological_processresponse to oxidative stress
A0007084biological_processmitotic nuclear membrane reassembly
A0009615biological_processresponse to virus
A0010836biological_processnegative regulation of protein ADP-ribosylation
A0015074biological_processDNA integration
A0032480biological_processnegative regulation of type I interferon production
A0042802molecular_functionidentical protein binding
A0042803molecular_functionprotein homodimerization activity
A0045071biological_processnegative regulation of viral genome replication
A0045824biological_processnegative regulation of innate immune response
A0051276biological_processchromosome organization
A0160049biological_processnegative regulation of cGAS/STING signaling pathway
C0000785cellular_componentchromatin
C0000793cellular_componentcondensed chromosome
C0003677molecular_functionDNA binding
C0003690molecular_functiondouble-stranded DNA binding
C0005515molecular_functionprotein binding
C0005634cellular_componentnucleus
C0005635cellular_componentnuclear envelope
C0005654cellular_componentnucleoplasm
C0005694cellular_componentchromosome
C0005737cellular_componentcytoplasm
C0005829cellular_componentcytosol
C0006325biological_processchromatin organization
C0006979biological_processresponse to oxidative stress
C0007084biological_processmitotic nuclear membrane reassembly
C0009615biological_processresponse to virus
C0010836biological_processnegative regulation of protein ADP-ribosylation
C0015074biological_processDNA integration
C0032480biological_processnegative regulation of type I interferon production
C0042802molecular_functionidentical protein binding
C0042803molecular_functionprotein homodimerization activity
C0045071biological_processnegative regulation of viral genome replication
C0045824biological_processnegative regulation of innate immune response
C0051276biological_processchromosome organization
C0160049biological_processnegative regulation of cGAS/STING signaling pathway
D0000785cellular_componentchromatin
D0000793cellular_componentcondensed chromosome
D0003677molecular_functionDNA binding
D0003690molecular_functiondouble-stranded DNA binding
D0005515molecular_functionprotein binding
D0005634cellular_componentnucleus
D0005635cellular_componentnuclear envelope
D0005654cellular_componentnucleoplasm
D0005694cellular_componentchromosome
D0005737cellular_componentcytoplasm
D0005829cellular_componentcytosol
D0006325biological_processchromatin organization
D0006979biological_processresponse to oxidative stress
D0007084biological_processmitotic nuclear membrane reassembly
D0009615biological_processresponse to virus
D0010836biological_processnegative regulation of protein ADP-ribosylation
D0015074biological_processDNA integration
D0032480biological_processnegative regulation of type I interferon production
D0042802molecular_functionidentical protein binding
D0042803molecular_functionprotein homodimerization activity
D0045071biological_processnegative regulation of viral genome replication
D0045824biological_processnegative regulation of innate immune response
D0051276biological_processchromosome organization
D0160049biological_processnegative regulation of cGAS/STING signaling pathway
E0000785cellular_componentchromatin
E0000793cellular_componentcondensed chromosome
E0003677molecular_functionDNA binding
E0003690molecular_functiondouble-stranded DNA binding
E0005515molecular_functionprotein binding
E0005634cellular_componentnucleus
E0005635cellular_componentnuclear envelope
E0005654cellular_componentnucleoplasm
E0005694cellular_componentchromosome
E0005737cellular_componentcytoplasm
E0005829cellular_componentcytosol
E0006325biological_processchromatin organization
E0006979biological_processresponse to oxidative stress
E0007084biological_processmitotic nuclear membrane reassembly
E0009615biological_processresponse to virus
E0010836biological_processnegative regulation of protein ADP-ribosylation
E0015074biological_processDNA integration
E0032480biological_processnegative regulation of type I interferon production
E0042802molecular_functionidentical protein binding
E0042803molecular_functionprotein homodimerization activity
E0045071biological_processnegative regulation of viral genome replication
E0045824biological_processnegative regulation of innate immune response
E0051276biological_processchromosome organization
E0160049biological_processnegative regulation of cGAS/STING signaling pathway
G0005635cellular_componentnuclear envelope
H0005635cellular_componentnuclear envelope
Functional Information from PDB Data
site_idAC1
Number of Residues5
Detailsbinding site for residue SO4 G 101
ChainResidue
FARG482
GARG17
GHIS23
GHOH201
GHOH206
site_idAC2
Number of Residues5
Detailsbinding site for residue SO4 D 101
ChainResidue
DGLN73
DGLY27
DGLU28
DVAL29
DLEU30
site_idAC3
Number of Residues2
Detailsbinding site for residue SO4 D 102
ChainResidue
DARG60
DARG75
site_idAC4
Number of Residues8
Detailsbinding site for residue SO4 E 101
ChainResidue
ESER4
ELYS6
EALA24
EGLY25
EASP76
EHOH207
EHOH211
EHOH222
site_idAC5
Number of Residues6
Detailsbinding site for residue SO4 E 102
ChainResidue
CGLY27
CGLU28
CVAL29
EARG60
EARG75
EHOH216
site_idAC6
Number of Residues5
Detailsbinding site for residue SO4 A 101
ChainResidue
ASER4
AALA24
AGLY25
AHOH203
AHOH221
site_idAC7
Number of Residues4
Detailsbinding site for residue EDO A 102
ChainResidue
AARG60
AARG75
DLYS6
DHOH203
site_idAC8
Number of Residues2
Detailsbinding site for residue SO4 C 101
ChainResidue
CARG60
CARG75
site_idAC9
Number of Residues5
Detailsbinding site for residue SO4 H 101
ChainResidue
BARG482
HARG17
HHIS23
HHOH201
HHOH208
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"20068231","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI2
Number of Residues2
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"24275569","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI3
Number of Residues60
DetailsDomain: {"description":"HhH","evidences":[{"source":"PubMed","id":"10924106","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI4
Number of Residues6
DetailsModified residue: {"description":"Phosphothreonine; by VRK1 and VRK2","evidences":[{"source":"PubMed","id":"16495336","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI5
Number of Residues4
DetailsModified residue: {"description":"Phosphoserine; by viral VacV B1 kinase, VRK1 and VRK2","evidences":[{"source":"PubMed","id":"16371512","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16495336","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI6
Number of Residues117
DetailsDomain: {"description":"LTD","evidences":[{"source":"PROSITE-ProRule","id":"PRU01187","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI7
Number of Residues4
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI8
Number of Residues2
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"20068231","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI9
Number of Residues2
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"19608861","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI10
Number of Residues4
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"P48678","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI11
Number of Residues2
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"24741066","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"18669648","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"20068231","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"21406692","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"24275569","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI12
Number of Residues2
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"20068231","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"24275569","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI13
Number of Residues4
DetailsModified residue: {"description":"Phosphothreonine","evidences":[{"source":"UniProtKB","id":"P48679","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI14
Number of Residues2
DetailsModified residue: {"description":"Phosphothreonine","evidences":[{"source":"PubMed","id":"20068231","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI15
Number of Residues2
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P48678","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI16
Number of Residues2
DetailsCross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate","evidences":[{"source":"PubMed","id":"28112733","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI17
Number of Residues6
DetailsCross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)","evidences":[{"source":"PubMed","id":"28112733","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

243911

PDB entries from 2025-10-29

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