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1KCW

X-RAY CRYSTAL STRUCTURE OF HUMAN CERULOPLASMIN AT 3.0 ANGSTROMS

Functional Information from GO Data
ChainGOidnamespacecontents
A0004322molecular_functionferroxidase activity
A0004602molecular_functionglutathione peroxidase activity
A0005507molecular_functioncopper ion binding
A0005576cellular_componentextracellular region
A0005615cellular_componentextracellular space
A0005765cellular_componentlysosomal membrane
A0005788cellular_componentendoplasmic reticulum lumen
A0005886cellular_componentplasma membrane
A0006811biological_processmonoatomic ion transport
A0006825biological_processcopper ion transport
A0006826biological_processiron ion transport
A0006878biological_processintracellular copper ion homeostasis
A0006879biological_processintracellular iron ion homeostasis
A0016491molecular_functionoxidoreductase activity
A0016724molecular_functionoxidoreductase activity, acting on metal ions, oxygen as acceptor
A0038023molecular_functionsignaling receptor activity
A0046872molecular_functionmetal ion binding
A0047066molecular_functionphospholipid-hydroperoxide glutathione peroxidase activity
A0051087molecular_functionprotein-folding chaperone binding
A0070062cellular_componentextracellular exosome
A0072562cellular_componentblood microparticle
A0098869biological_processcellular oxidant detoxification
Functional Information from PDB Data
site_idCU1
Number of Residues5
DetailsTYPE I CU BINDING SITE IN DOMAIN 2. AT BEST LEU 329 MAY HAVE VAN DER WAALS CONTACT WITH THE CU.
ChainResidue
ACU1049
AHIS276
ACYS319
AHIS324
ALEU329

site_idCU2
Number of Residues5
DetailsTYPE I CU BINDING SITE IN DOMAIN 4.
ChainResidue
AMET690
ACU1053
AHIS637
ACYS680
AHIS685

site_idCU3
Number of Residues5
DetailsLABILE CU BINDING SITE IN DOMAIN 4.
ChainResidue
ACU1054
AGLU597
AHIS602
AASP684
AGLU971

site_idCU4
Number of Residues5
DetailsTYPE I CU BINDING SITE IN DOMAIN 6.
ChainResidue
ACU1055
AHIS975
ACYS1021
AHIS1026
AMET1031

site_idCU5
Number of Residues5
DetailsLABILE CU BINDING SITE IN DOMAIN 6.
ChainResidue
ACU1056
AGLU272
AGLU935
AHIS940
AASP1025

site_idTRI
Number of Residues13
DetailsTRINUCLEAR CENTER. CU31 AND 32 ARE THE PAIR OF TYPE III CU AND CU34 IS THE TYPE II CU. O33 BRIDGES CU 31 - 32 AND O35 BRIDGES Y 107 - CU 34.
ChainResidue
ACU1050
ACU1051
AO1057
ACU1052
AO1058
AHIS101
AHIS103
AHIS161
AHIS163
AHIS978
AHIS980
AHIS1020
AHIS1022

Functional Information from PROSITE/UniProt
site_idPS00079
Number of Residues21
DetailsMULTICOPPER_OXIDASE1 Multicopper oxidases signature 1. GeWmLsCqNLnhLkAGLqafF
ChainResidueDetails
AGLY313-PHE333
AGLY674-TYR694
AGLY1015-TYR1035

site_idPS00080
Number of Residues12
DetailsMULTICOPPER_OXIDASE2 Multicopper oxidases signature 2. HCHvtdHihaGM
ChainResidueDetails
AHIS1020-MET1031

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsBINDING: type 2 copper site
ChainResidueDetails
AHIS101
AHIS978

site_idSWS_FT_FI2
Number of Residues6
DetailsBINDING: type 3 copper site
ChainResidueDetails
AHIS103
AHIS161
AHIS163
AHIS980
AHIS1020
AHIS1022

site_idSWS_FT_FI3
Number of Residues11
DetailsBINDING: type 1 copper site
ChainResidueDetails
AHIS276
AHIS1026
AMET1031
ACYS319
AHIS324
AHIS637
ACYS680
AHIS685
AMET690
AHIS975
ACYS1021

site_idSWS_FT_FI4
Number of Residues1
DetailsMOD_RES: Phosphoserine; by FAM20C => ECO:0000269|PubMed:26091039
ChainResidueDetails
ASER703

site_idSWS_FT_FI5
Number of Residues1
DetailsCARBOHYD: N-linked (GlcNAc...) (complex) asparagine => ECO:0000269|PubMed:14760718, ECO:0000269|PubMed:15084671, ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:19139490, ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:19838169
ChainResidueDetails
AASN119

site_idSWS_FT_FI6
Number of Residues1
DetailsCARBOHYD: N-linked (GlcNAc...) (complex) asparagine => ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:19139490, ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:19838169
ChainResidueDetails
AASN339

site_idSWS_FT_FI7
Number of Residues1
DetailsCARBOHYD: N-linked (GlcNAc...) (complex) asparagine => ECO:0000269|PubMed:14760718, ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:19139490, ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:19838169
ChainResidueDetails
AASN378

site_idSWS_FT_FI8
Number of Residues2
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:16335952
ChainResidueDetails
AASN569
AASN907

site_idSWS_FT_FI9
Number of Residues1
DetailsCARBOHYD: N-linked (GlcNAc...) (complex) asparagine => ECO:0000269|PubMed:14760718, ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:19139490, ECO:0000269|PubMed:19159218
ChainResidueDetails
AASN743

217705

数据于2024-03-27公开中

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