1KCW

X-RAY CRYSTAL STRUCTURE OF HUMAN CERULOPLASMIN AT 3.0 ANGSTROMS

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Functional Information from GO Data

ChainGOidnamespacecontents
A0072562cellular_componentblood microparticle
A0005788cellular_componentendoplasmic reticulum lumen
A0070062cellular_componentextracellular exosome
A0005576cellular_componentextracellular region
A0005615cellular_componentextracellular space
A0005765cellular_componentlysosomal membrane
A0005886cellular_componentplasma membrane
A0051087molecular_functionchaperone binding
A0005507molecular_functioncopper ion binding
A0004322molecular_functionferroxidase activity
A0016491molecular_functionoxidoreductase activity
A0006879biological_processcellular iron ion homeostasis
A0044267biological_processcellular protein metabolic process
A0006825biological_processcopper ion transport
A0055072biological_processiron ion homeostasis
A0006826biological_processiron ion transport
A0043687biological_processpost-translational protein modification
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Functional Information from PDB Data

site_idNumber of ResiduesDetails
CU15TYPE 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

CU25TYPE I CU BINDING SITE IN DOMAIN 4.
ChainResidue
ACU1053
AHIS637
ACYS680
AHIS685
AMET690

CU35LABILE CU BINDING SITE IN DOMAIN 4.
ChainResidue
ACU1054
AGLU597
AHIS602
AASP684
AGLU971

CU45TYPE I CU BINDING SITE IN DOMAIN 6.
ChainResidue
ACU1055
AHIS975
ACYS1021
AHIS1026
AMET1031

CU55LABILE CU BINDING SITE IN DOMAIN 6.
ChainResidue
ACU1056
AGLU272
AGLU935
AHIS940
AASP1025

TRI13TRINUCLEAR 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

AC12BINDING SITE FOR RESIDUE NAG A 1047
ChainResidue
AASN119
AILE1016

AC21BINDING SITE FOR RESIDUE NAG A 1048
ChainResidue
AASN743

AC33BINDING SITE FOR RESIDUE CU A 1049
ChainResidue
AHIS276
ACYS319
AHIS324

AC45BINDING SITE FOR RESIDUE CU A 1050
ChainResidue
AHIS163
AHIS980
AHIS1020
ACU1051
AO1057

AC56BINDING SITE FOR RESIDUE CU A 1051
ChainResidue
AHIS103
AHIS161
AHIS1022
ACU1050
ACU1052
AO1057

AC67BINDING SITE FOR RESIDUE CU A 1052
ChainResidue
AHIS101
AHIS103
AHIS978
AHIS980
ACU1051
AO1057
AO1058

AC74BINDING SITE FOR RESIDUE CU A 1053
ChainResidue
AHIS637
ACYS680
AHIS685
AMET690

AC82BINDING SITE FOR RESIDUE CU A 1054
ChainResidue
AHIS602
AASP684

AC95BINDING SITE FOR RESIDUE CU A 1055
ChainResidue
ALEU974
AHIS975
ACYS1021
AHIS1026
AMET1031

BC13BINDING SITE FOR RESIDUE CU A 1056
ChainResidue
AGLU935
AHIS940
AASP1025

BC210BINDING SITE FOR RESIDUE O A 1057
ChainResidue
AHIS103
AHIS161
AHIS163
AHIS978
AHIS980
AHIS1020
AHIS1022
ACU1050
ACU1051
ACU1052

BC37BINDING SITE FOR RESIDUE O A 1058
ChainResidue
AHIS101
ASER102
AHIS103
ATYR107
AHIS978
AHIS980
ACU1052

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Functional Information from PDB atom coordinates for the "HETATM" binding sites

site_idNumber of ResiduesDetails
NAG_1kcw_A_10475N-ACETYL-D-GLUCOSAMINE binding site
ChainResidueligand
APRO117NAG: N-ACETYL-D-GLUCOSAMINE
AASN119NAG: N-ACETYL-D-GLUCOSAMINE
AGLU735NAG: N-ACETYL-D-GLUCOSAMINE
AILE1016NAG: N-ACETYL-D-GLUCOSAMINE
ATHR1034NAG: N-ACETYL-D-GLUCOSAMINE

NAG_1kcw_A_10481N-ACETYL-D-GLUCOSAMINE binding site
ChainResidueligand
AASN743NAG: N-ACETYL-D-GLUCOSAMINE

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Functional Information from PROSITE/UniProt

site_idNumber of ResiduesDetails
PS0007963Multicopper oxidases signature 1. G-x-[FYW]-x-[LIVMFYW]-x-[CST]-x-{PR}-{K}-x(2)-{S}-x-{LFH}-G-[LM]-x(3)
ChainResidueDetails
AGLY313-PHE333
AGLY674-TYR694
AGLY1015-TYR1035

PS0008012Multicopper oxidases signature 2. H-C-H-x(3)-H-x(3)-[AG]-[LM]
ChainResidueDetails
AHIS1020-MET1031

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Functional Information from SwissProt/UniProt

site_idNumber of ResiduesDetails
SWS_FT_FI13Copper 3; type 3
ChainResidueDetails
AHIS163
AHIS980
AHIS1020

SWS_FT_FI24Copper 6; type 1
ChainResidueDetails
AHIS975
ACYS1021
AHIS1026
AMET1031

SWS_FT_FI33Copper 2; type 3
ChainResidueDetails
AHIS103
AHIS161
AHIS1022

SWS_FT_FI44Copper 5; type 1
ChainResidueDetails
AHIS637
ACYS680
AHIS685
AMET690

SWS_FT_FI53Copper 4; type 1
ChainResidueDetails
AHIS276
ACYS319
AHIS324

SWS_FT_FI62Copper 1; type 2
ChainResidueDetails
AHIS101
AHIS978

CSA13Annotated By Reference To The Literature 1a65
ChainResidueDetails
AHIS1020
AHIS1022
ACYS1021

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Catalytic Information from CSA

site_idNumber of ResiduesDetails
CSA13Annotated By Reference To The Literature 1a65
ChainResidueDetails
AHIS1020
AHIS1022
ACYS1021