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6I7S

Microsomal triglyceride transfer protein

Functional Information from GO Data
ChainGOidnamespacecontents
A0003723molecular_functionRNA binding
A0003756molecular_functionprotein disulfide isomerase activity
A0003779molecular_functionactin binding
A0004656molecular_functionprocollagen-proline 4-dioxygenase activity
A0005178molecular_functionintegrin binding
A0005515molecular_functionprotein binding
A0005576cellular_componentextracellular region
A0005783cellular_componentendoplasmic reticulum
A0005788cellular_componentendoplasmic reticulum lumen
A0005793cellular_componentendoplasmic reticulum-Golgi intermediate compartment
A0005829cellular_componentcytosol
A0005856cellular_componentcytoskeleton
A0005886cellular_componentplasma membrane
A0005925cellular_componentfocal adhesion
A0006457biological_processprotein folding
A0009897cellular_componentexternal side of plasma membrane
A0015035molecular_functionprotein-disulfide reductase activity
A0016222cellular_componentprocollagen-proline 4-dioxygenase complex
A0016853molecular_functionisomerase activity
A0016972molecular_functionthiol oxidase activity
A0018401biological_processpeptidyl-proline hydroxylation to 4-hydroxy-L-proline
A0019899molecular_functionenzyme binding
A0030027cellular_componentlamellipodium
A0030070biological_processinsulin processing
A0032991cellular_componentprotein-containing complex
A0034663cellular_componentendoplasmic reticulum chaperone complex
A0034975biological_processprotein folding in endoplasmic reticulum
A0034976biological_processresponse to endoplasmic reticulum stress
A0035722biological_processinterleukin-12-mediated signaling pathway
A0038155biological_processinterleukin-23-mediated signaling pathway
A0042470cellular_componentmelanosome
A0044877molecular_functionprotein-containing complex binding
A0045785biological_processpositive regulation of cell adhesion
A0046598biological_processpositive regulation of viral entry into host cell
A0046982molecular_functionprotein heterodimerization activity
A0070062cellular_componentextracellular exosome
A0071456biological_processcellular response to hypoxia
A1900026biological_processpositive regulation of substrate adhesion-dependent cell spreading
A1902175biological_processregulation of oxidative stress-induced intrinsic apoptotic signaling pathway
A2000406biological_processpositive regulation of T cell migration
B0003723molecular_functionRNA binding
B0003756molecular_functionprotein disulfide isomerase activity
B0003779molecular_functionactin binding
B0004656molecular_functionprocollagen-proline 4-dioxygenase activity
B0005178molecular_functionintegrin binding
B0005515molecular_functionprotein binding
B0005576cellular_componentextracellular region
B0005783cellular_componentendoplasmic reticulum
B0005788cellular_componentendoplasmic reticulum lumen
B0005793cellular_componentendoplasmic reticulum-Golgi intermediate compartment
B0005829cellular_componentcytosol
B0005856cellular_componentcytoskeleton
B0005886cellular_componentplasma membrane
B0005925cellular_componentfocal adhesion
B0006457biological_processprotein folding
B0009897cellular_componentexternal side of plasma membrane
B0015035molecular_functionprotein-disulfide reductase activity
B0016222cellular_componentprocollagen-proline 4-dioxygenase complex
B0016853molecular_functionisomerase activity
B0016972molecular_functionthiol oxidase activity
B0018401biological_processpeptidyl-proline hydroxylation to 4-hydroxy-L-proline
B0019899molecular_functionenzyme binding
B0030027cellular_componentlamellipodium
B0030070biological_processinsulin processing
B0032991cellular_componentprotein-containing complex
B0034663cellular_componentendoplasmic reticulum chaperone complex
B0034975biological_processprotein folding in endoplasmic reticulum
B0034976biological_processresponse to endoplasmic reticulum stress
B0035722biological_processinterleukin-12-mediated signaling pathway
B0038155biological_processinterleukin-23-mediated signaling pathway
B0042470cellular_componentmelanosome
B0044877molecular_functionprotein-containing complex binding
B0045785biological_processpositive regulation of cell adhesion
B0046598biological_processpositive regulation of viral entry into host cell
B0046982molecular_functionprotein heterodimerization activity
B0070062cellular_componentextracellular exosome
B0071456biological_processcellular response to hypoxia
B1900026biological_processpositive regulation of substrate adhesion-dependent cell spreading
B1902175biological_processregulation of oxidative stress-induced intrinsic apoptotic signaling pathway
B2000406biological_processpositive regulation of T cell migration
G0005319molecular_functionlipid transporter activity
G0005515molecular_functionprotein binding
G0005548molecular_functionphospholipid transporter activity
G0005783cellular_componentendoplasmic reticulum
G0005788cellular_componentendoplasmic reticulum lumen
G0005794cellular_componentGolgi apparatus
G0006629biological_processlipid metabolic process
G0006869biological_processlipid transport
G0007623biological_processcircadian rhythm
G0008289molecular_functionlipid binding
G0009306biological_processprotein secretion
G0015914biological_processphospholipid transport
G0015918biological_processsterol transport
G0016323cellular_componentbasolateral plasma membrane
G0031526cellular_componentbrush border membrane
G0031528cellular_componentmicrovillus membrane
G0031982cellular_componentvesicle
G0034185molecular_functionapolipoprotein binding
G0034197biological_processtriglyceride transport
G0034377biological_processplasma lipoprotein particle assembly
G0034378biological_processchylomicron assembly
G0034379biological_processvery-low-density lipoprotein particle assembly
G0042157biological_processlipoprotein metabolic process
G0042632biological_processcholesterol homeostasis
G0043235cellular_componentreceptor complex
G0044877molecular_functionprotein-containing complex binding
G0046982molecular_functionprotein heterodimerization activity
G0051592biological_processresponse to calcium ion
G0120009biological_processintermembrane lipid transfer
G0120014molecular_functionphospholipid transfer activity
G0120019molecular_functionphosphatidylcholine transfer activity
G0120020molecular_functioncholesterol transfer activity
G0140344molecular_functiontriglyceride transfer activity
G1902388molecular_functionceramide 1-phosphate transfer activity
G1902389biological_processceramide 1-phosphate transport
G1904121molecular_functionphosphatidylethanolamine transfer activity
H0005319molecular_functionlipid transporter activity
H0005515molecular_functionprotein binding
H0005548molecular_functionphospholipid transporter activity
H0005783cellular_componentendoplasmic reticulum
H0005788cellular_componentendoplasmic reticulum lumen
H0005794cellular_componentGolgi apparatus
H0006629biological_processlipid metabolic process
H0006869biological_processlipid transport
H0007623biological_processcircadian rhythm
H0008289molecular_functionlipid binding
H0009306biological_processprotein secretion
H0015914biological_processphospholipid transport
H0015918biological_processsterol transport
H0016323cellular_componentbasolateral plasma membrane
H0031526cellular_componentbrush border membrane
H0031528cellular_componentmicrovillus membrane
H0031982cellular_componentvesicle
H0034185molecular_functionapolipoprotein binding
H0034197biological_processtriglyceride transport
H0034377biological_processplasma lipoprotein particle assembly
H0034378biological_processchylomicron assembly
H0034379biological_processvery-low-density lipoprotein particle assembly
H0042157biological_processlipoprotein metabolic process
H0042632biological_processcholesterol homeostasis
H0043235cellular_componentreceptor complex
H0044877molecular_functionprotein-containing complex binding
H0046982molecular_functionprotein heterodimerization activity
H0051592biological_processresponse to calcium ion
H0120009biological_processintermembrane lipid transfer
H0120014molecular_functionphospholipid transfer activity
H0120019molecular_functionphosphatidylcholine transfer activity
H0120020molecular_functioncholesterol transfer activity
H0140344molecular_functiontriglyceride transfer activity
H1902388molecular_functionceramide 1-phosphate transfer activity
H1902389biological_processceramide 1-phosphate transport
H1904121molecular_functionphosphatidylethanolamine transfer activity
Functional Information from PDB Data
site_idAC1
Number of Residues5
Detailsbinding site for residue CA A 601
ChainResidue
AALA381
AASP383
ALYS386
APHE446
APRO447

site_idAC2
Number of Residues3
Detailsbinding site for residue EDO A 602
ChainResidue
ALYS162
ASER190
AASP199

site_idAC3
Number of Residues6
Detailsbinding site for residue EDO A 603
ChainResidue
ASER153
AGLU154
APHE206
ALYS207
ALYS208
AVAL150

site_idAC4
Number of Residues1
Detailsbinding site for residue EDO A 604
ChainResidue
ALYS276

site_idAC5
Number of Residues3
Detailsbinding site for residue EDO A 605
ChainResidue
ALYS415
AHOH714
GLYS195

site_idAC6
Number of Residues1
Detailsbinding site for residue EDO A 606
ChainResidue
AGLY349

site_idAC7
Number of Residues5
Detailsbinding site for residue CA B 601
ChainResidue
BALA381
BASP383
BLYS386
BPHE446
BPRO447

site_idAC8
Number of Residues2
Detailsbinding site for residue PGE B 602
ChainResidue
BALA118
BARG120

site_idAC9
Number of Residues5
Detailsbinding site for residue PGE B 603
ChainResidue
BTYR327
BGLY349
GLYS103
GLYS105
GLYS109

site_idAD1
Number of Residues6
Detailsbinding site for residue SO4 B 604
ChainResidue
BGLU322
BGLU323
BMET324
BHOH708
HARG594
HHIS603

site_idAD2
Number of Residues2
Detailsbinding site for residue EDO B 605
ChainResidue
BVAL237
BLYS276

site_idAD3
Number of Residues3
Detailsbinding site for residue EDO B 606
ChainResidue
BTYR49
BCYS56
BLYS81

site_idAD4
Number of Residues2
Detailsbinding site for residue EDO B 607
ChainResidue
BASN419
GLYS278

site_idAD5
Number of Residues3
Detailsbinding site for residue PEG B 608
ChainResidue
BGLU177
BALA178
BLYS222

site_idAD6
Number of Residues3
Detailsbinding site for residue PEG B 609
ChainResidue
BHIS438
GGLN95
HHOH1039

site_idAD7
Number of Residues5
Detailsbinding site for residue PE5 G 901
ChainResidue
GSER646
GSER662
GASN780
GALA809
GPHE813

site_idAD8
Number of Residues4
Detailsbinding site for residue PGE G 902
ChainResidue
GGLU391
GTYR395
GVAL728
GHOH1003

site_idAD9
Number of Residues1
Detailsbinding site for residue TRS G 903
ChainResidue
GVAL227

site_idAE1
Number of Residues3
Detailsbinding site for residue SO4 G 904
ChainResidue
GGLY850
GARG851
GGLY852

site_idAE2
Number of Residues5
Detailsbinding site for residue SO4 G 905
ChainResidue
GGLU90
GASN91
GPHE102
GHOH1006
GHOH1012

site_idAE3
Number of Residues4
Detailsbinding site for residue SO4 G 906
ChainResidue
GGLU536
GLYS537
GTHR538
GARG644

site_idAE4
Number of Residues4
Detailsbinding site for residue SO4 G 907
ChainResidue
GSER39
GARG58
GLYS255
GHOH1016

site_idAE5
Number of Residues6
Detailsbinding site for residue SO4 G 908
ChainResidue
GSER768
GLEU769
GTRP770
HILE196
HALA197
HARG198

site_idAE6
Number of Residues4
Detailsbinding site for residue SO4 G 909
ChainResidue
AARG300
GGLN569
GARG610
GSER611

site_idAE7
Number of Residues2
Detailsbinding site for residue SO4 G 910
ChainResidue
GILE188
GALA190

site_idAE8
Number of Residues1
Detailsbinding site for residue EDO G 911
ChainResidue
GARG623

site_idAE9
Number of Residues1
Detailsbinding site for residue EDO G 912
ChainResidue
GARG121

site_idAF1
Number of Residues2
Detailsbinding site for residue EDO G 913
ChainResidue
GASN140
GGLU141

site_idAF2
Number of Residues2
Detailsbinding site for residue EDO G 914
ChainResidue
GSER296
GLYS748

site_idAF3
Number of Residues2
Detailsbinding site for residue EDO G 915
ChainResidue
GARG312
GASN352

site_idAF4
Number of Residues9
Detailsbinding site for residue EDO G 916
ChainResidue
GPHE399
GALA400
GSER401
GILE732
GLEU733
GHOH1011
GSER365
GGLN367
GALA396

site_idAF5
Number of Residues4
Detailsbinding site for residue PEG G 918
ChainResidue
GGLN509
GASN549
GHIS660
GGLN663

site_idAF6
Number of Residues4
Detailsbinding site for residue PE5 H 901
ChainResidue
HSER646
HSER662
HASN780
HPHE813

site_idAF7
Number of Residues8
Detailsbinding site for residue PE4 H 902
ChainResidue
HLYS99
HTHR849
HGLY850
HARG851
HGLY852
HVAL854
HGLN856
HHOH1055

site_idAF8
Number of Residues5
Detailsbinding site for residue PGE H 903
ChainResidue
HGLN509
HARG510
HTYR511
HASP512
HPHE651

site_idAF9
Number of Residues1
Detailsbinding site for residue PGE H 904
ChainResidue
HTYR554

site_idAG1
Number of Residues3
Detailsbinding site for residue PGE H 905
ChainResidue
HSER27
HPHE226
HVAL227

site_idAG2
Number of Residues4
Detailsbinding site for residue SO4 H 906
ChainResidue
GARG32
GALA263
HTHR517
HASP518

site_idAG3
Number of Residues4
Detailsbinding site for residue SO4 H 907
ChainResidue
HGLN569
HARG610
HSER611
HHOH1005

site_idAG4
Number of Residues3
Detailsbinding site for residue SO4 H 908
ChainResidue
HGLN530
HARG540
HPRO568

site_idAG5
Number of Residues2
Detailsbinding site for residue EDO H 909
ChainResidue
HTHR705
HHOH1040

site_idAG6
Number of Residues2
Detailsbinding site for residue EDO H 910
ChainResidue
HARG312
HASN352

site_idAG7
Number of Residues3
Detailsbinding site for residue EDO H 911
ChainResidue
HPRO204
HASN205
HGLN441

site_idAG8
Number of Residues1
Detailsbinding site for residue EDO H 912
ChainResidue
HTYR314

site_idAG9
Number of Residues2
Detailsbinding site for residue EDO H 913
ChainResidue
HTHR165
HASN166

site_idAH1
Number of Residues5
Detailsbinding site for residue PEG H 914
ChainResidue
HTYR395
HPHE399
HLEU701
HVAL728
HGLY730

site_idAH2
Number of Residues1
Detailsbinding site for residue PEG H 915
ChainResidue
HMET692

site_idAH3
Number of Residues2
Detailsbinding site for residue PEG H 916
ChainResidue
GSER269
HLYS859

site_idAH4
Number of Residues5
Detailsbinding site for residue PEG H 917
ChainResidue
HTHR37
HTYR38
HSER39
HSER61
HLYS255

site_idAH5
Number of Residues1
Detailsbinding site for residue PEG H 918
ChainResidue
HGLY200

Functional Information from PROSITE/UniProt
site_idPS00014
Number of Residues4
DetailsER_TARGET Endoplasmic reticulum targeting sequence. KDEL
ChainResidueDetails
ALYS505-LEU508

site_idPS00194
Number of Residues19
DetailsTHIOREDOXIN_1 Thioredoxin family active site. LVeFYapWCGHCKaLapeY
ChainResidueDetails
ALEU45-TYR63
APHE389-TRP407

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues252
DetailsDomain: {"description":"Thioredoxin 2","evidences":[{"source":"PROSITE-ProRule","id":"PRU00691","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues4
DetailsActive site: {"description":"Nucleophile"}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues4
DetailsActive site: {"description":"Nucleophile","evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues4
DetailsSite: {"description":"Contributes to redox potential value"}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues2
DetailsSite: {"description":"Lowers pKa of C-terminal Cys of first active site"}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues4
DetailsSite: {"description":"Contributes to redox potential value","evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues2
DetailsSite: {"description":"Lowers pKa of C-terminal Cys of second active site","evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues2
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"P09103","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI9
Number of Residues4
DetailsModified residue: {"description":"N6-succinyllysine","evidences":[{"source":"UniProtKB","id":"P09103","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI10
Number of Residues4
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"32149426","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI11
Number of Residues2
DetailsModified residue: {"description":"Phosphoserine; by FAM20C","evidences":[{"source":"PubMed","id":"26091039","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"32149426","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI12
Number of Residues1262
DetailsDomain: {"description":"Vitellogenin","evidences":[{"source":"PROSITE-ProRule","id":"PRU00557","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idMCSA1
Number of Residues4
DetailsM-CSA 191
ChainResidueDetails
ACYS53nucleofuge, nucleophile, proton acceptor, proton donor
AGLY54activator, modifies pKa
AHIS55modifies pKa, proton acceptor, proton donor
ACYS56

site_idMCSA2
Number of Residues4
DetailsM-CSA 191
ChainResidueDetails
BCYS53nucleofuge, nucleophile, proton acceptor, proton donor
BGLY54activator, modifies pKa
BHIS55modifies pKa, proton acceptor, proton donor
BCYS56

248335

PDB entries from 2026-01-28

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