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4EJX

Structure of ceruloplasmin-myeloperoxidase complex

Functional Information from GO Data
ChainGOidnamespacecontents
A0005507molecular_functioncopper ion binding
A0016491molecular_functionoxidoreductase activity
B0004601molecular_functionperoxidase activity
B0006979biological_processresponse to oxidative stress
B0020037molecular_functionheme binding
D0004601molecular_functionperoxidase activity
D0006979biological_processresponse to oxidative stress
D0020037molecular_functionheme binding
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

site_idPS00435
Number of Residues11
DetailsPEROXIDASE_1 Peroxidases proximal heme-ligand signature. EMPELTSMHTL
ChainResidueDetails
DGLU242-LEU252

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsBINDING: BINDING => ECO:0000269|PubMed:10766826, ECO:0000269|PubMed:11705390, ECO:0000269|PubMed:7840679, ECO:0007744|PDB:1CXP, ECO:0007744|PDB:1D2V, ECO:0007744|PDB:1D7W, ECO:0007744|PDB:1DNU, ECO:0007744|PDB:1DNW, ECO:0007744|PDB:1MHL
ChainResidueDetails
DTHR168
DPHE170
DASP172
DSER174

site_idSWS_FT_FI2
Number of Residues2
DetailsBINDING: covalent => ECO:0000269|PubMed:23843990, ECO:0000269|PubMed:7840679, ECO:0007744|PDB:1CXP, ECO:0007744|PDB:4EJX
ChainResidueDetails
DGLU242
DMET243
ATYR48
ALYS109
AGLN124
AASP127
AASP128
ASER237

site_idSWS_FT_FI3
Number of Residues1
DetailsBINDING: axial binding residue => ECO:0000269|PubMed:23843990, ECO:0000269|PubMed:7840679, ECO:0007744|PDB:1CXP, ECO:0007744|PDB:4EJX
ChainResidueDetails
DHIS336
AHIS978

site_idSWS_FT_FI4
Number of Residues1
DetailsSITE: Transition state stabilizer
ChainResidueDetails
DARG239
AHIS161
AHIS163
AHIS980
AHIS1020
AHIS1022

site_idSWS_FT_FI5
Number of Residues1
DetailsMOD_RES: Cysteine sulfenic acid (-SOH) => ECO:0000269|PubMed:7840679
ChainResidueDetails
DCYS150
ACYS319
AHIS324
AHIS637
ACYS680
AHIS685
AMET690
AHIS1026
AMET1031

site_idSWS_FT_FI6
Number of Residues1
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:16740002, ECO:0000269|PubMed:20332087
ChainResidueDetails
DASN157
AGLY398
ATYR401
ASER598
APHE748
AGLY757
ATYR760
ASER936

site_idSWS_FT_FI7
Number of Residues2
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:20332087, ECO:0000269|PubMed:23843990, ECO:0007744|PDB:4EJX
ChainResidueDetails
DASN189
DASN225

site_idSWS_FT_FI8
Number of Residues1
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:16740002, ECO:0000269|PubMed:20332087, ECO:0000269|PubMed:23843990, ECO:0007744|PDB:4EJX
ChainResidueDetails
DASN317

site_idSWS_FT_FI9
Number of Residues1
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:20332087
ChainResidueDetails
DASN563

site_idSWS_FT_FI10
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_FI11
Number of Residues1
DetailsCARBOHYD: N-linked (GlcNAc...) (complex) asparagine => ECO:0000269|PubMed:14760718, ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:17242517, ECO:0000269|PubMed:19139490, ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:19838169, ECO:0000269|PubMed:23843990, ECO:0007744|PDB:2J5W, ECO:0007744|PDB:4EJX, ECO:0007744|PDB:4ENZ
ChainResidueDetails
AASN378

site_idSWS_FT_FI12
Number of Residues2
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:16335952
ChainResidueDetails
AASN569
AASN907

site_idSWS_FT_FI13
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|Ref.29, ECO:0007744|PDB:1KCW
ChainResidueDetails
AASN743

Catalytic Information from CSA
site_idMCSA1
Number of Residues1
DetailsM-CSA 601
ChainResidueDetails
DARG239electrostatic stabiliser

222926

PDB entries from 2024-07-24

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