eF-site ID 4ejx-A
PDB Code 4ejx
Chain A

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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
Description


Functional site
1) chain A
residue 313-333
type prosite
sequence GEWMLSCQNLNHLKAGLQAFF
description MULTICOPPER_OXIDASE1 Multicopper oxidases signature 1. GeWmLsCqNLnhLkAGLqafF
source prosite : PS00079
2) chain A
residue 674-694
type prosite
sequence GTFNVECLTTDHYTGGMKQKY
description MULTICOPPER_OXIDASE1 Multicopper oxidases signature 1. GeWmLsCqNLnhLkAGLqafF
source prosite : PS00079
3) chain A
residue 1015-1035
type prosite
sequence GIWLLHCHVTDHIHAGMETTY
description MULTICOPPER_OXIDASE1 Multicopper oxidases signature 1. GeWmLsCqNLnhLkAGLqafF
source prosite : PS00079
4) chain A
residue 1020-1031
type prosite
sequence HCHVTDHIHAGM
description MULTICOPPER_OXIDASE2 Multicopper oxidases signature 2. HCHvtdHihaGM
source prosite : PS00080
5) chain A
residue 339
type CARBOHYD
sequence N
description N-linked (GlcNAc...) (complex) asparagine => ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:19139490, ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:19838169
source Swiss-Prot : SWS_FT_FI10
6) 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_FI11
7) chain A
residue 569
type CARBOHYD
sequence N
description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:16335952
source Swiss-Prot : SWS_FT_FI12
8) chain A
residue 907
type CARBOHYD
sequence N
description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:16335952
source Swiss-Prot : SWS_FT_FI12
9) 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.29, ECO:0007744|PDB:1KCW
source Swiss-Prot : SWS_FT_FI13
10) chain A
residue 237
type BINDING
sequence S
description covalent => ECO:0000269|PubMed:23843990, ECO:0000269|PubMed:7840679, ECO:0007744|PDB:1CXP, ECO:0007744|PDB:4EJX
source Swiss-Prot : SWS_FT_FI2
11) chain A
residue 978
type BINDING
sequence H
description covalent => ECO:0000269|PubMed:23843990, ECO:0000269|PubMed:7840679, ECO:0007744|PDB:1CXP, ECO:0007744|PDB:4EJX
source Swiss-Prot : SWS_FT_FI2
12) chain A
residue 1022
type BINDING
sequence H
description covalent => ECO:0000269|PubMed:23843990, ECO:0000269|PubMed:7840679, ECO:0007744|PDB:1CXP, ECO:0007744|PDB:4EJX
source Swiss-Prot : SWS_FT_FI2
13) chain A
residue 48
type BINDING
sequence Y
description covalent => ECO:0000269|PubMed:23843990, ECO:0000269|PubMed:7840679, ECO:0007744|PDB:1CXP, ECO:0007744|PDB:4EJX
source Swiss-Prot : SWS_FT_FI2
14) chain A
residue 101
type BINDING
sequence H
description covalent => ECO:0000269|PubMed:23843990, ECO:0000269|PubMed:7840679, ECO:0007744|PDB:1CXP, ECO:0007744|PDB:4EJX
source Swiss-Prot : SWS_FT_FI2
15) chain A
residue 109
type BINDING
sequence K
description covalent => ECO:0000269|PubMed:23843990, ECO:0000269|PubMed:7840679, ECO:0007744|PDB:1CXP, ECO:0007744|PDB:4EJX
source Swiss-Prot : SWS_FT_FI2
16) chain A
residue 124
type BINDING
sequence Q
description covalent => ECO:0000269|PubMed:23843990, ECO:0000269|PubMed:7840679, ECO:0007744|PDB:1CXP, ECO:0007744|PDB:4EJX
source Swiss-Prot : SWS_FT_FI2
17) chain A
residue 127
type BINDING
sequence D
description covalent => ECO:0000269|PubMed:23843990, ECO:0000269|PubMed:7840679, ECO:0007744|PDB:1CXP, ECO:0007744|PDB:4EJX
source Swiss-Prot : SWS_FT_FI2
18) chain A
residue 128
type BINDING
sequence D
description covalent => ECO:0000269|PubMed:23843990, ECO:0000269|PubMed:7840679, ECO:0007744|PDB:1CXP, ECO:0007744|PDB:4EJX
source Swiss-Prot : SWS_FT_FI2
19) chain A
residue 161
type BINDING
sequence H
description covalent => ECO:0000269|PubMed:23843990, ECO:0000269|PubMed:7840679, ECO:0007744|PDB:1CXP, ECO:0007744|PDB:4EJX
source Swiss-Prot : SWS_FT_FI2
20) 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
21) 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
22) chain A
residue 319
type SITE
sequence C
description Transition state stabilizer
source Swiss-Prot : SWS_FT_FI4
23) chain A
residue 324
type SITE
sequence H
description Transition state stabilizer
source Swiss-Prot : SWS_FT_FI4
24) chain A
residue 637
type SITE
sequence H
description Transition state stabilizer
source Swiss-Prot : SWS_FT_FI4
25) chain A
residue 680
type SITE
sequence C
description Transition state stabilizer
source Swiss-Prot : SWS_FT_FI4
26) chain A
residue 685
type SITE
sequence H
description Transition state stabilizer
source Swiss-Prot : SWS_FT_FI4
27) chain A
residue 690
type SITE
sequence M
description Transition state stabilizer
source Swiss-Prot : SWS_FT_FI4
28) chain A
residue 1026
type SITE
sequence H
description Transition state stabilizer
source Swiss-Prot : SWS_FT_FI4
29) chain A
residue 1031
type SITE
sequence M
description Transition state stabilizer
source Swiss-Prot : SWS_FT_FI4
30) chain A
residue 398
type MOD_RES
sequence G
description Cysteine sulfenic acid (-SOH) => ECO:0000269|PubMed:7840679
source Swiss-Prot : SWS_FT_FI5
31) chain A
residue 401
type MOD_RES
sequence Y
description Cysteine sulfenic acid (-SOH) => ECO:0000269|PubMed:7840679
source Swiss-Prot : SWS_FT_FI5
32) chain A
residue 598
type MOD_RES
sequence S
description Cysteine sulfenic acid (-SOH) => ECO:0000269|PubMed:7840679
source Swiss-Prot : SWS_FT_FI5
33) chain A
residue 748
type MOD_RES
sequence F
description Cysteine sulfenic acid (-SOH) => ECO:0000269|PubMed:7840679
source Swiss-Prot : SWS_FT_FI5
34) chain A
residue 757
type MOD_RES
sequence G
description Cysteine sulfenic acid (-SOH) => ECO:0000269|PubMed:7840679
source Swiss-Prot : SWS_FT_FI5
35) chain A
residue 760
type MOD_RES
sequence Y
description Cysteine sulfenic acid (-SOH) => ECO:0000269|PubMed:7840679
source Swiss-Prot : SWS_FT_FI5
36) chain A
residue 936
type MOD_RES
sequence S
description Cysteine sulfenic acid (-SOH) => ECO:0000269|PubMed:7840679
source Swiss-Prot : SWS_FT_FI5
37) 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

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