eF-site ID 4ejx-ABD
PDB Code 4ejx
Chain A, B, D

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Title Structure of ceruloplasmin-myeloperoxidase complex
Classification OXIDOREDUCTASE
Compound Ceruloplasmin
Source ORGANISM_COMMON: human; ORGANISM_SCIENTIFIC: Homo sapiens;
Sequence A:  KEKHYYIGIIETTWDYASDHGEKKLISVDTEHSNIYLQNG
PDRIGRLYKKALYLQYTDETFRTTIEKPVWLGFLGPIIKA
ETGDKVYVHLKNLASRPYTFHSHGITYYKEHEGAIYPDNT
TDFQRADDKVYPGEQYTYMLLATEEQSPGEGDGNCVTRIY
HSHIDAPKDIASGLIGPLIICKKDSLDKEKEKHIDREFVV
MFSVVDENFSWYLEDNIKTYCSEPEKVDKDNEDFQQSNRM
YSVNGYTFGSLSGLSMCAEDRVKWYLFGMGNEVDVHAAFF
HGQALTNKNYRIDTINLFPATLFDAYMVAQNPGEWMLSCQ
NLNHLKAGLQAFFQVQECNKSSSKDNIRGKHVRHYYIAAE
EIIWNYAPSGIDIFTKENLTAPGSDSAVFFEQGTTRIGGS
YKKLVYREYTDASFTNRKERGPEEEHLGILGPVIWAEVGD
TIRVTFHNKGAYPLSIEPIGVRFNKNNEGTYYSPNVPPSA
SHVAPTETFTYEWTVPKEVGPTNADPVCLAKMYYSAVDPT
KDIFTGLIGPMKICKKGSLHANGRQKDVDKEFYLFPTVFD
ENESLLLEDNIRMFTTAPDQVDKEDEDFQESNKMHSMNGF
MYGNQPGLTMCKGDSVVWYLFSAGNEADVHGIYFSGNTYL
WRGERRDTANLFPQTSLTLHMWPDTEGTFNVECLTTDHYT
GGMKQKYTVNQCRRQSEDSTFYLGERTYYIAAVEVEWDYS
PQREWEKELHHLQEQNVSNAFLDKGEFYIGSKYKKVVYRQ
YTDSTFRVPVERKAEEEHLGILGPQLHADVGDKVKIIFKN
MATRPYSIHAHGVQTESSTVTPTLPGETLTYVWKIPERSG
AGTEDSACIPWAYYSTVDQVKDLYSGLIGPLIVCRRPYLK
VFNPRRKLEFALLFLVFDENESWYLDDNIKTYSDHPEKVN
KDDEEFIESNKMHAINGRMFGNLQGLTMHVGDEVNWYLMG
MGNEIDLHTVHFHGHSFQYKHRGVYSSDVFDIFPGTYQTL
EMFPRTPGIWLLHCHVTDHIHAGMETTYTVLQNE
B:  CPEQDKYRTITGMCNNRRSPTLGASNRAFVRWLPAEYEDG
FSLPYGWTPGVKRNGFPVALARAVSNEIVRFPTDQLTPDQ
ERSLMFMQWGQLLDHDLDFTPEPA
D:  VNCETSCVQQPPCFPLKIPPNDPRIKNQADCIPFFRSCPA
CPGSNITIRNQINALTSFVDASMVYGSEEPLARNLRNMSN
QLGLLAVNQRFQDNGRALLPFDNLHDDPCLLTNRSARIPC
FLAGDTRSSEMPELTSMHTLLLREHNRLATELKSLNPRWD
GERLYQEARKIVGAMVQIITYRDYLPLVLGPTAMRKYLPT
YRSYNDSVDPRIANVFTNAFRYGHTLIQPFMFRLDNRYQP
MEPNPRVPLSRVFFASWRVVLEGGIDPILRGLMATPAKLN
RQNQIAVDEIRERLFEQVMRIGLDLPALNMQRSRDHGLPG
YNAWRRFCGLPQPETVGQLGTVLRNLKLARKLMEQYGTPN
NIDIWMGGVSEPLKRKGRVGPLLACIIGTQFRKLRDGDRF
WWENEGVFSMQQRQALAQISLPRIICDNTGITTVSKNNIF
MSNSYPRDFVNCSTLPALNLASWREA
Description


Functional site
1) chain D
residue 239
type catalytic
sequence R
description 601
source MCSA : MCSA1
2) chain D
residue 242-252
type prosite
sequence EMPELTSMHTL
description PEROXIDASE_1 Peroxidases proximal heme-ligand signature. EMPELTSMHTL
source prosite : PS00435
3) chain A
residue 1020-1031
type prosite
sequence HCHVTDHIHAGM
description MULTICOPPER_OXIDASE2 Multicopper oxidases signature 2. HCHvtdHihaGM
source prosite : PS00080
4) chain A
residue 313-333
type prosite
sequence GEWMLSCQNLNHLKAGLQAFF
description MULTICOPPER_OXIDASE1 Multicopper oxidases signature 1. GeWmLsCqNLnhLkAGLqafF
source prosite : PS00079
5) chain A
residue 674-694
type prosite
sequence GTFNVECLTTDHYTGGMKQKY
description MULTICOPPER_OXIDASE1 Multicopper oxidases signature 1. GeWmLsCqNLnhLkAGLqafF
source prosite : PS00079
6) chain A
residue 1015-1035
type prosite
sequence GIWLLHCHVTDHIHAGMETTY
description MULTICOPPER_OXIDASE1 Multicopper oxidases signature 1. GeWmLsCqNLnhLkAGLqafF
source prosite : PS00079
7) chain D
residue 150
type MOD_RES
sequence C
description Cysteine sulfenic acid (-SOH) => ECO:0000269|PubMed:7840679
source Swiss-Prot : SWS_FT_FI5
8) chain A
residue 398
type MOD_RES
sequence G
description Cysteine sulfenic acid (-SOH) => ECO:0000269|PubMed:7840679
source Swiss-Prot : SWS_FT_FI5
9) chain A
residue 401
type MOD_RES
sequence Y
description Cysteine sulfenic acid (-SOH) => ECO:0000269|PubMed:7840679
source Swiss-Prot : SWS_FT_FI5
10) chain A
residue 598
type MOD_RES
sequence S
description Cysteine sulfenic acid (-SOH) => ECO:0000269|PubMed:7840679
source Swiss-Prot : SWS_FT_FI5
11) chain A
residue 748
type MOD_RES
sequence F
description Cysteine sulfenic acid (-SOH) => ECO:0000269|PubMed:7840679
source Swiss-Prot : SWS_FT_FI5
12) chain A
residue 757
type MOD_RES
sequence G
description Cysteine sulfenic acid (-SOH) => ECO:0000269|PubMed:7840679
source Swiss-Prot : SWS_FT_FI5
13) chain A
residue 760
type MOD_RES
sequence Y
description Cysteine sulfenic acid (-SOH) => ECO:0000269|PubMed:7840679
source Swiss-Prot : SWS_FT_FI5
14) chain A
residue 936
type MOD_RES
sequence S
description Cysteine sulfenic acid (-SOH) => ECO:0000269|PubMed:7840679
source Swiss-Prot : SWS_FT_FI5
15) chain D
residue 157
type CARBOHYD
sequence N
description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:16740002, ECO:0000269|PubMed:20332087
source Swiss-Prot : SWS_FT_FI6
16) chain A
residue 1021
type CARBOHYD
sequence C
description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:16740002, ECO:0000269|PubMed:20332087
source Swiss-Prot : SWS_FT_FI6
17) chain D
residue 563
type CARBOHYD
sequence N
description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:20332087
source Swiss-Prot : SWS_FT_FI9
18) chain D
residue 239
type SITE
sequence R
description Transition state stabilizer
source Swiss-Prot : SWS_FT_FI4
19) chain A
residue 319
type SITE
sequence C
description Transition state stabilizer
source Swiss-Prot : SWS_FT_FI4
20) chain A
residue 324
type SITE
sequence H
description Transition state stabilizer
source Swiss-Prot : SWS_FT_FI4
21) chain A
residue 637
type SITE
sequence H
description Transition state stabilizer
source Swiss-Prot : SWS_FT_FI4
22) chain A
residue 680
type SITE
sequence C
description Transition state stabilizer
source Swiss-Prot : SWS_FT_FI4
23) chain A
residue 685
type SITE
sequence H
description Transition state stabilizer
source Swiss-Prot : SWS_FT_FI4
24) chain A
residue 690
type SITE
sequence M
description Transition state stabilizer
source Swiss-Prot : SWS_FT_FI4
25) chain A
residue 1026
type SITE
sequence H
description Transition state stabilizer
source Swiss-Prot : SWS_FT_FI4
26) chain A
residue 1031
type SITE
sequence M
description Transition state stabilizer
source Swiss-Prot : SWS_FT_FI4
27) chain A
residue 378
type CARBOHYD
sequence N
description 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
source Swiss-Prot : SWS_FT_FI10
28) chain A
residue 569
type CARBOHYD
sequence N
description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:16335952
source Swiss-Prot : SWS_FT_FI11
29) chain A
residue 907
type CARBOHYD
sequence N
description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:16335952
source Swiss-Prot : SWS_FT_FI11
30) chain A
residue 743
type CARBOHYD
sequence N
description N-linked (GlcNAc...) (complex) asparagine => ECO:0000269|PubMed:14760718, ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:19139490, ECO:0000269|PubMed:19159218, ECO:0000269|Ref.27, ECO:0007744|PDB:1KCW
source Swiss-Prot : SWS_FT_FI12
31) chain D
residue 168
type BINDING
sequence T
description 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
source Swiss-Prot : SWS_FT_FI1
32) chain D
residue 170
type BINDING
sequence F
description 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
source Swiss-Prot : SWS_FT_FI1
33) chain D
residue 172
type BINDING
sequence D
description 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
source Swiss-Prot : SWS_FT_FI1
34) chain D
residue 174
type BINDING
sequence S
description 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
source Swiss-Prot : SWS_FT_FI1
35) chain A
residue 124
type BINDING
sequence Q
description 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
source Swiss-Prot : SWS_FT_FI1
36) chain A
residue 127
type BINDING
sequence D
description 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
source Swiss-Prot : SWS_FT_FI1
37) chain A
residue 128
type BINDING
sequence D
description 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
source Swiss-Prot : SWS_FT_FI1
38) chain A
residue 237
type BINDING
sequence S
description 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
source Swiss-Prot : SWS_FT_FI1
39) chain D
residue 336
type BINDING
sequence H
description axial binding residue => ECO:0000269|PubMed:23843990, ECO:0000269|PubMed:7840679, ECO:0007744|PDB:1CXP, ECO:0007744|PDB:4EJX
source Swiss-Prot : SWS_FT_FI3
40) chain A
residue 161
type BINDING
sequence H
description axial binding residue => ECO:0000269|PubMed:23843990, ECO:0000269|PubMed:7840679, ECO:0007744|PDB:1CXP, ECO:0007744|PDB:4EJX
source Swiss-Prot : SWS_FT_FI3
41) chain A
residue 163
type BINDING
sequence H
description axial binding residue => ECO:0000269|PubMed:23843990, ECO:0000269|PubMed:7840679, ECO:0007744|PDB:1CXP, ECO:0007744|PDB:4EJX
source Swiss-Prot : SWS_FT_FI3
42) chain A
residue 980
type BINDING
sequence H
description axial binding residue => ECO:0000269|PubMed:23843990, ECO:0000269|PubMed:7840679, ECO:0007744|PDB:1CXP, ECO:0007744|PDB:4EJX
source Swiss-Prot : SWS_FT_FI3
43) chain A
residue 1020
type BINDING
sequence H
description axial binding residue => ECO:0000269|PubMed:23843990, ECO:0000269|PubMed:7840679, ECO:0007744|PDB:1CXP, ECO:0007744|PDB:4EJX
source Swiss-Prot : SWS_FT_FI3
44) chain A
residue 1022
type BINDING
sequence H
description axial binding residue => ECO:0000269|PubMed:23843990, ECO:0000269|PubMed:7840679, ECO:0007744|PDB:1CXP, ECO:0007744|PDB:4EJX
source Swiss-Prot : SWS_FT_FI3
45) chain D
residue 189
type CARBOHYD
sequence N
description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:20332087, ECO:0000269|PubMed:23843990, ECO:0007744|PDB:4EJX
source Swiss-Prot : SWS_FT_FI7
46) chain D
residue 225
type CARBOHYD
sequence N
description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:20332087, ECO:0000269|PubMed:23843990, ECO:0007744|PDB:4EJX
source Swiss-Prot : SWS_FT_FI7
47) chain D
residue 317
type CARBOHYD
sequence N
description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:16740002, ECO:0000269|PubMed:20332087, ECO:0000269|PubMed:23843990, ECO:0007744|PDB:4EJX
source Swiss-Prot : SWS_FT_FI8
48) chain D
residue 242
type BINDING
sequence E
description covalent => ECO:0000269|PubMed:23843990, ECO:0000269|PubMed:7840679, ECO:0007744|PDB:1CXP, ECO:0007744|PDB:4EJX
source Swiss-Prot : SWS_FT_FI2
49) chain D
residue 243
type BINDING
sequence M
description covalent => ECO:0000269|PubMed:23843990, ECO:0000269|PubMed:7840679, ECO:0007744|PDB:1CXP, ECO:0007744|PDB:4EJX
source Swiss-Prot : SWS_FT_FI2

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