eF-site ID 2j5w-A
PDB Code 2j5w
Chain A

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Title Ceruloplasmin revisited: structural and functional roles of various metal cation binding sites
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
AGTEDSACIPWAYYSTVDQVKDLYSGLIGPLIVCRRPNPR
RKLEFALLFLVFDENESWYLDDNIKTYSDHPEKVNKDDEE
FIESNKMHAINGRMFGNLQGLTMHVGDEVNWYLMGMGNEI
DLHTVHFHGHSFQYKHRGVYSSDVFDIFPGTYQTLEMFPR
TPGIWLLHCHVTDHIHAGMETTYTVLQNE
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 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
5) chain A
residue 569
type CARBOHYD
sequence N
description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:16335952
source Swiss-Prot : SWS_FT_FI11
6) chain A
residue 907
type CARBOHYD
sequence N
description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:16335952
source Swiss-Prot : SWS_FT_FI11
7) 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
8) chain A
residue 48
type BINDING
sequence Y
description BINDING => ECO:0000269|PubMed:17242517, ECO:0000269|PubMed:23843990, ECO:0007744|PDB:2J5W, ECO:0007744|PDB:4ENZ
source Swiss-Prot : SWS_FT_FI1
9) chain A
residue 109
type BINDING
sequence K
description BINDING => ECO:0000269|PubMed:17242517, ECO:0000269|PubMed:23843990, ECO:0007744|PDB:2J5W, ECO:0007744|PDB:4ENZ
source Swiss-Prot : SWS_FT_FI1
10) chain A
residue 124
type BINDING
sequence Q
description BINDING => ECO:0000269|PubMed:17242517, ECO:0000269|PubMed:23843990, ECO:0007744|PDB:2J5W, ECO:0007744|PDB:4ENZ
source Swiss-Prot : SWS_FT_FI1
11) chain A
residue 127
type BINDING
sequence D
description BINDING => ECO:0000269|PubMed:17242517, ECO:0000269|PubMed:23843990, ECO:0007744|PDB:2J5W, ECO:0007744|PDB:4ENZ
source Swiss-Prot : SWS_FT_FI1
12) chain A
residue 128
type BINDING
sequence D
description BINDING => ECO:0000269|PubMed:17242517, ECO:0000269|PubMed:23843990, ECO:0007744|PDB:2J5W, ECO:0007744|PDB:4ENZ
source Swiss-Prot : SWS_FT_FI1
13) chain A
residue 237
type BINDING
sequence S
description BINDING => ECO:0000269|PubMed:17242517, ECO:0000269|PubMed:23843990, ECO:0007744|PDB:2J5W, ECO:0007744|PDB:4ENZ
source Swiss-Prot : SWS_FT_FI1
14) chain A
residue 36
type BINDING
sequence Y
description BINDING => ECO:0000269|PubMed:17242517, ECO:0000269|PubMed:23843990, ECO:0007744|PDB:2J5W, ECO:0007744|PDB:4ENZ
source Swiss-Prot : SWS_FT_FI1
15) chain A
residue 45
type BINDING
sequence G
description BINDING => ECO:0000269|PubMed:17242517, ECO:0000269|PubMed:23843990, ECO:0007744|PDB:2J5W, ECO:0007744|PDB:4ENZ
source Swiss-Prot : SWS_FT_FI1
16) chain A
residue 101
type BINDING
sequence H
description type 2 copper site => ECO:0000269|PubMed:17242517, ECO:0000269|PubMed:23843990, ECO:0000269|Ref.27, ECO:0007744|PDB:1KCW, ECO:0007744|PDB:2J5W, ECO:0007744|PDB:4EJX, ECO:0007744|PDB:4ENZ
source Swiss-Prot : SWS_FT_FI2
17) chain A
residue 978
type BINDING
sequence H
description type 2 copper site => ECO:0000269|PubMed:17242517, ECO:0000269|PubMed:23843990, ECO:0000269|Ref.27, ECO:0007744|PDB:1KCW, ECO:0007744|PDB:2J5W, ECO:0007744|PDB:4EJX, ECO:0007744|PDB:4ENZ
source Swiss-Prot : SWS_FT_FI2
18) chain A
residue 103
type BINDING
sequence H
description type 3 copper site => ECO:0000269|PubMed:17242517, ECO:0000269|PubMed:23843990, ECO:0000269|Ref.27, ECO:0007744|PDB:1KCW, ECO:0007744|PDB:2J5W, ECO:0007744|PDB:4EJX, ECO:0007744|PDB:4ENZ
source Swiss-Prot : SWS_FT_FI3
19) chain A
residue 161
type BINDING
sequence H
description type 3 copper site => ECO:0000269|PubMed:17242517, ECO:0000269|PubMed:23843990, ECO:0000269|Ref.27, ECO:0007744|PDB:1KCW, ECO:0007744|PDB:2J5W, ECO:0007744|PDB:4EJX, ECO:0007744|PDB:4ENZ
source Swiss-Prot : SWS_FT_FI3
20) chain A
residue 163
type BINDING
sequence H
description type 3 copper site => ECO:0000269|PubMed:17242517, ECO:0000269|PubMed:23843990, ECO:0000269|Ref.27, ECO:0007744|PDB:1KCW, ECO:0007744|PDB:2J5W, ECO:0007744|PDB:4EJX, ECO:0007744|PDB:4ENZ
source Swiss-Prot : SWS_FT_FI3
21) chain A
residue 980
type BINDING
sequence H
description type 3 copper site => ECO:0000269|PubMed:17242517, ECO:0000269|PubMed:23843990, ECO:0000269|Ref.27, ECO:0007744|PDB:1KCW, ECO:0007744|PDB:2J5W, ECO:0007744|PDB:4EJX, ECO:0007744|PDB:4ENZ
source Swiss-Prot : SWS_FT_FI3
22) chain A
residue 1020
type BINDING
sequence H
description type 3 copper site => ECO:0000269|PubMed:17242517, ECO:0000269|PubMed:23843990, ECO:0000269|Ref.27, ECO:0007744|PDB:1KCW, ECO:0007744|PDB:2J5W, ECO:0007744|PDB:4EJX, ECO:0007744|PDB:4ENZ
source Swiss-Prot : SWS_FT_FI3
23) chain A
residue 1022
type BINDING
sequence H
description type 3 copper site => ECO:0000269|PubMed:17242517, ECO:0000269|PubMed:23843990, ECO:0000269|Ref.27, ECO:0007744|PDB:1KCW, ECO:0007744|PDB:2J5W, ECO:0007744|PDB:4EJX, ECO:0007744|PDB:4ENZ
source Swiss-Prot : SWS_FT_FI3
24) chain A
residue 319
type BINDING
sequence C
description type 1 copper site => ECO:0000269|PubMed:17242517, ECO:0000269|PubMed:23843990, ECO:0000269|Ref.27, ECO:0007744|PDB:1KCW, ECO:0007744|PDB:2J5W, ECO:0007744|PDB:4ENZ
source Swiss-Prot : SWS_FT_FI4
25) chain A
residue 324
type BINDING
sequence H
description type 1 copper site => ECO:0000269|PubMed:17242517, ECO:0000269|PubMed:23843990, ECO:0000269|Ref.27, ECO:0007744|PDB:1KCW, ECO:0007744|PDB:2J5W, ECO:0007744|PDB:4ENZ
source Swiss-Prot : SWS_FT_FI4
26) chain A
residue 637
type BINDING
sequence H
description type 1 copper site => ECO:0000269|PubMed:17242517, ECO:0000269|PubMed:23843990, ECO:0000269|Ref.27, ECO:0007744|PDB:1KCW, ECO:0007744|PDB:2J5W, ECO:0007744|PDB:4ENZ
source Swiss-Prot : SWS_FT_FI4
27) chain A
residue 680
type BINDING
sequence C
description type 1 copper site => ECO:0000269|PubMed:17242517, ECO:0000269|PubMed:23843990, ECO:0000269|Ref.27, ECO:0007744|PDB:1KCW, ECO:0007744|PDB:2J5W, ECO:0007744|PDB:4ENZ
source Swiss-Prot : SWS_FT_FI4
28) chain A
residue 685
type BINDING
sequence H
description type 1 copper site => ECO:0000269|PubMed:17242517, ECO:0000269|PubMed:23843990, ECO:0000269|Ref.27, ECO:0007744|PDB:1KCW, ECO:0007744|PDB:2J5W, ECO:0007744|PDB:4ENZ
source Swiss-Prot : SWS_FT_FI4
29) chain A
residue 690
type BINDING
sequence M
description type 1 copper site => ECO:0000269|PubMed:17242517, ECO:0000269|PubMed:23843990, ECO:0000269|Ref.27, ECO:0007744|PDB:1KCW, ECO:0007744|PDB:2J5W, ECO:0007744|PDB:4ENZ
source Swiss-Prot : SWS_FT_FI4
30) chain A
residue 1026
type BINDING
sequence H
description type 1 copper site => ECO:0000269|PubMed:17242517, ECO:0000269|PubMed:23843990, ECO:0000269|Ref.27, ECO:0007744|PDB:1KCW, ECO:0007744|PDB:2J5W, ECO:0007744|PDB:4ENZ
source Swiss-Prot : SWS_FT_FI4
31) chain A
residue 1031
type BINDING
sequence M
description type 1 copper site => ECO:0000269|PubMed:17242517, ECO:0000269|PubMed:23843990, ECO:0000269|Ref.27, ECO:0007744|PDB:1KCW, ECO:0007744|PDB:2J5W, ECO:0007744|PDB:4ENZ
source Swiss-Prot : SWS_FT_FI4
32) chain A
residue 276
type BINDING
sequence H
description type 1 copper site => ECO:0000269|PubMed:17242517, ECO:0000269|PubMed:23843990, ECO:0000269|Ref.27, ECO:0007744|PDB:1KCW, ECO:0007744|PDB:2J5W, ECO:0007744|PDB:4ENZ
source Swiss-Prot : SWS_FT_FI4
33) chain A
residue 1021
type BINDING
sequence C
description type 1 copper site => ECO:0000269|PubMed:17242517, ECO:0000269|PubMed:23843990, ECO:0000269|Ref.27, ECO:0007744|PDB:1KCW, ECO:0007744|PDB:2J5W, ECO:0007744|PDB:4EJX, ECO:0007744|PDB:4ENZ
source Swiss-Prot : SWS_FT_FI6
34) chain A
residue 975
type BINDING
sequence H
description type 1 copper site => ECO:0000269|PubMed:17242517, ECO:0000269|PubMed:23843990, ECO:0000269|Ref.27, ECO:0007744|PDB:1KCW, ECO:0007744|PDB:2J5W, ECO:0007744|PDB:4EJX, ECO:0007744|PDB:4ENZ
source Swiss-Prot : SWS_FT_FI6
35) chain A
residue 703
type MOD_RES
sequence S
description Phosphoserine; by FAM20C => ECO:0000269|PubMed:26091039
source Swiss-Prot : SWS_FT_FI7
36) chain A
residue 119
type CARBOHYD
sequence N
description N-linked (GlcNAc...) (complex) asparagine => ECO:0000269|PubMed:14760718, ECO:0000269|PubMed:15084671, 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:0000269|Ref.27, ECO:0007744|PDB:1KCW, ECO:0007744|PDB:2J5W, ECO:0007744|PDB:4EJX, ECO:0007744|PDB:4ENZ
source Swiss-Prot : SWS_FT_FI8
37) 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_FI9
38) chain A
residue 1020-1031
type prosite
sequence HCHVTDHIHAGM
description MULTICOPPER_OXIDASE2 Multicopper oxidases signature 2. HCHvtdHihaGM
source prosite : PS00080
39) chain A
residue 398
type BINDING
sequence G
description BINDING => ECO:0000269|PubMed:17242517, ECO:0007744|PDB:2J5W
source Swiss-Prot : SWS_FT_FI5
40) chain A
residue 401
type BINDING
sequence Y
description BINDING => ECO:0000269|PubMed:17242517, ECO:0007744|PDB:2J5W
source Swiss-Prot : SWS_FT_FI5
41) chain A
residue 598
type BINDING
sequence S
description BINDING => ECO:0000269|PubMed:17242517, ECO:0007744|PDB:2J5W
source Swiss-Prot : SWS_FT_FI5
42) chain A
residue 748
type BINDING
sequence F
description BINDING => ECO:0000269|PubMed:17242517, ECO:0007744|PDB:2J5W
source Swiss-Prot : SWS_FT_FI5
43) chain A
residue 757
type BINDING
sequence G
description BINDING => ECO:0000269|PubMed:17242517, ECO:0007744|PDB:2J5W
source Swiss-Prot : SWS_FT_FI5
44) chain A
residue 760
type BINDING
sequence Y
description BINDING => ECO:0000269|PubMed:17242517, ECO:0007744|PDB:2J5W
source Swiss-Prot : SWS_FT_FI5
45) chain A
residue 936
type BINDING
sequence S
description BINDING => ECO:0000269|PubMed:17242517, ECO:0007744|PDB:2J5W
source Swiss-Prot : SWS_FT_FI5
46) chain A
residue 389
type BINDING
sequence F
description BINDING => ECO:0000269|PubMed:17242517, ECO:0007744|PDB:2J5W
source Swiss-Prot : SWS_FT_FI5

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