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3KJY

Crystal structure of reduced HOMO SAPIENS CLIC3

Functional Information from GO Data
ChainGOidnamespacecontents
A0005254molecular_functionchloride channel activity
A0005515molecular_functionprotein binding
A0005576cellular_componentextracellular region
A0005634cellular_componentnucleus
A0005737cellular_componentcytoplasm
A0005886cellular_componentplasma membrane
A0006821biological_processchloride transport
A0007165biological_processsignal transduction
A0016020cellular_componentmembrane
A0016491molecular_functionoxidoreductase activity
A0016604cellular_componentnuclear body
A0019153molecular_functionprotein-disulfide reductase (glutathione) activity
A0031012cellular_componentextracellular matrix
A0034220biological_processmonoatomic ion transmembrane transport
A0034707cellular_componentchloride channel complex
A0070062cellular_componentextracellular exosome
A1902476biological_processchloride transmembrane transport
A1903672biological_processpositive regulation of sprouting angiogenesis
B0005254molecular_functionchloride channel activity
B0005515molecular_functionprotein binding
B0005576cellular_componentextracellular region
B0005634cellular_componentnucleus
B0005737cellular_componentcytoplasm
B0005886cellular_componentplasma membrane
B0006821biological_processchloride transport
B0007165biological_processsignal transduction
B0016020cellular_componentmembrane
B0016491molecular_functionoxidoreductase activity
B0016604cellular_componentnuclear body
B0019153molecular_functionprotein-disulfide reductase (glutathione) activity
B0031012cellular_componentextracellular matrix
B0034220biological_processmonoatomic ion transmembrane transport
B0034707cellular_componentchloride channel complex
B0070062cellular_componentextracellular exosome
B1902476biological_processchloride transmembrane transport
B1903672biological_processpositive regulation of sprouting angiogenesis
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE SO4 A 231
ChainResidue
AARG27
ALEU76
AHOH239
AHOH265
BLYS111
BGLN130

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 A 232
ChainResidue
BALA197
BGLU198
AHIS221
ASER222
BPRO196

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 A 233
ChainResidue
ALYS111
AHOH236
BARG27
BLEU76

site_idAC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE SO4 A 234
ChainResidue
AARG97
AHIS148
AGLY166
AASP167
AARG168
AHOH253

site_idAC5
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 A 235
ChainResidue
APHE109
AHIS110
ALYS179
AHOH245
BHIS110

site_idAC6
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 B 231
ChainResidue
AHIS110
BHIS110
BLYS179
BHOH250

site_idAC7
Number of Residues3
DetailsBINDING SITE FOR RESIDUE SO4 B 232
ChainResidue
BARG133
BARG137
BHOH289

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues40
DetailsTRANSMEM: Helical => ECO:0000255
ChainResidueDetails
ASER24-VAL44
BSER24-VAL44

site_idSWS_FT_FI2
Number of Residues4
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:23186163
ChainResidueDetails
ASER49
ASER159
BSER49
BSER159

Catalytic Information from CSA
site_idCSA1
Number of Residues1
DetailsAnnotated By Reference To The Literature 1oe8
ChainResidueDetails
AVAL10

site_idCSA2
Number of Residues1
DetailsAnnotated By Reference To The Literature 1oe8
ChainResidueDetails
BVAL10

223532

PDB entries from 2024-08-07

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