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SummaryStructural detailsExperimental detailsFunctional detailsSequence NeighborHistoryDownloads

7ZSC

Crystal structure of the heterodimeric human C-P4H-II with truncated alpha subunit (C-P4H-II delta281)

Functional Information from GO Data
ChainGOidnamespacecontents
A0005506molecular_functioniron ion binding
A0016705molecular_functionoxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen
A0031418molecular_functionL-ascorbic acid binding
B0005506molecular_functioniron ion binding
B0016705molecular_functionoxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen
B0031418molecular_functionL-ascorbic acid binding
C0003723molecular_functionRNA binding
C0003756molecular_functionprotein disulfide isomerase activity
C0003779molecular_functionactin binding
C0004656molecular_functionprocollagen-proline 4-dioxygenase activity
C0005178molecular_functionintegrin binding
C0005515molecular_functionprotein binding
C0005576cellular_componentextracellular region
C0005783cellular_componentendoplasmic reticulum
C0005788cellular_componentendoplasmic reticulum lumen
C0005793cellular_componentendoplasmic reticulum-Golgi intermediate compartment
C0005829cellular_componentcytosol
C0005856cellular_componentcytoskeleton
C0005886cellular_componentplasma membrane
C0005925cellular_componentfocal adhesion
C0006457biological_processprotein folding
C0009897cellular_componentexternal side of plasma membrane
C0015035molecular_functionprotein-disulfide reductase activity
C0016222cellular_componentprocollagen-proline 4-dioxygenase complex
C0016853molecular_functionisomerase activity
C0016972molecular_functionthiol oxidase activity
C0018401biological_processpeptidyl-proline hydroxylation to 4-hydroxy-L-proline
C0019899molecular_functionenzyme binding
C0030027cellular_componentlamellipodium
C0030070biological_processinsulin processing
C0032991cellular_componentprotein-containing complex
C0034663cellular_componentendoplasmic reticulum chaperone complex
C0034975biological_processprotein folding in endoplasmic reticulum
C0034976biological_processresponse to endoplasmic reticulum stress
C0035722biological_processinterleukin-12-mediated signaling pathway
C0038155biological_processinterleukin-23-mediated signaling pathway
C0042470cellular_componentmelanosome
C0044877molecular_functionprotein-containing complex binding
C0045785biological_processpositive regulation of cell adhesion
C0046598biological_processpositive regulation of viral entry into host cell
C0046982molecular_functionprotein heterodimerization activity
C0070062cellular_componentextracellular exosome
C0071456biological_processcellular response to hypoxia
C1900026biological_processpositive regulation of substrate adhesion-dependent cell spreading
C1902175biological_processregulation of oxidative stress-induced intrinsic apoptotic signaling pathway
C2000406biological_processpositive regulation of T cell migration
D0003723molecular_functionRNA binding
D0003756molecular_functionprotein disulfide isomerase activity
D0003779molecular_functionactin binding
D0004656molecular_functionprocollagen-proline 4-dioxygenase activity
D0005178molecular_functionintegrin binding
D0005515molecular_functionprotein binding
D0005576cellular_componentextracellular region
D0005783cellular_componentendoplasmic reticulum
D0005788cellular_componentendoplasmic reticulum lumen
D0005793cellular_componentendoplasmic reticulum-Golgi intermediate compartment
D0005829cellular_componentcytosol
D0005856cellular_componentcytoskeleton
D0005886cellular_componentplasma membrane
D0005925cellular_componentfocal adhesion
D0006457biological_processprotein folding
D0009897cellular_componentexternal side of plasma membrane
D0015035molecular_functionprotein-disulfide reductase activity
D0016222cellular_componentprocollagen-proline 4-dioxygenase complex
D0016853molecular_functionisomerase activity
D0016972molecular_functionthiol oxidase activity
D0018401biological_processpeptidyl-proline hydroxylation to 4-hydroxy-L-proline
D0019899molecular_functionenzyme binding
D0030027cellular_componentlamellipodium
D0030070biological_processinsulin processing
D0032991cellular_componentprotein-containing complex
D0034663cellular_componentendoplasmic reticulum chaperone complex
D0034975biological_processprotein folding in endoplasmic reticulum
D0034976biological_processresponse to endoplasmic reticulum stress
D0035722biological_processinterleukin-12-mediated signaling pathway
D0038155biological_processinterleukin-23-mediated signaling pathway
D0042470cellular_componentmelanosome
D0044877molecular_functionprotein-containing complex binding
D0045785biological_processpositive regulation of cell adhesion
D0046598biological_processpositive regulation of viral entry into host cell
D0046982molecular_functionprotein heterodimerization activity
D0070062cellular_componentextracellular exosome
D0071456biological_processcellular response to hypoxia
D1900026biological_processpositive regulation of substrate adhesion-dependent cell spreading
D1902175biological_processregulation of oxidative stress-induced intrinsic apoptotic signaling pathway
D2000406biological_processpositive regulation of T cell migration
Functional Information from PROSITE/UniProt
site_idPS00014
Number of Residues4
DetailsER_TARGET Endoplasmic reticulum targeting sequence. KDEL
ChainResidueDetails
CLYS505-LEU508
site_idPS00194
Number of Residues19
DetailsTHIOREDOXIN_1 Thioredoxin family active site. LVeFYapWCGHCKaLapeY
ChainResidueDetails
CLEU45-TYR63
CPHE389-TRP407
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues216
DetailsDomain: {"description":"Fe2OG dioxygenase","evidences":[{"source":"PROSITE-ProRule","id":"PRU00805","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI2
Number of Residues8
DetailsBinding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00805","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI3
Number of Residues2
DetailsModified residue: {"description":"N6-succinyllysine","evidences":[{"source":"UniProtKB","id":"Q60716","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI4
Number of Residues252
DetailsDomain: {"description":"Thioredoxin 2","evidences":[{"source":"PROSITE-ProRule","id":"PRU00691","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI5
Number of Residues4
DetailsActive site: {"description":"Nucleophile"}
ChainResidueDetails
site_idSWS_FT_FI6
Number of Residues4
DetailsActive site: {"description":"Nucleophile","evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI7
Number of Residues4
DetailsSite: {"description":"Contributes to redox potential value"}
ChainResidueDetails
site_idSWS_FT_FI8
Number of Residues2
DetailsSite: {"description":"Lowers pKa of C-terminal Cys of first active site"}
ChainResidueDetails
site_idSWS_FT_FI9
Number of Residues4
DetailsSite: {"description":"Contributes to redox potential value","evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI10
Number of Residues2
DetailsSite: {"description":"Lowers pKa of C-terminal Cys of second active site","evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI11
Number of Residues2
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"P09103","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI12
Number of Residues4
DetailsModified residue: {"description":"N6-succinyllysine","evidences":[{"source":"UniProtKB","id":"P09103","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI13
Number of Residues4
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"32149426","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI14
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
Catalytic Information from CSA
site_idMCSA1
Number of Residues4
DetailsM-CSA 191
ChainResidueDetails
CCYS53nucleofuge, nucleophile, proton acceptor, proton donor
CGLY54activator, modifies pKa
CHIS55modifies pKa, proton acceptor, proton donor
CCYS56
site_idMCSA2
Number of Residues4
DetailsM-CSA 191
ChainResidueDetails
DCYS53nucleofuge, nucleophile, proton acceptor, proton donor
DGLY54activator, modifies pKa
DHIS55modifies pKa, proton acceptor, proton donor
DCYS56

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PDB entries from 2025-12-17

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