eF-site ID 5wob-ABCDEFGHIJKLMNOPQRSTUVWXabcdefgh
PDB Code 5wob
Chain A, B, C, D, E, F, G, H, I, J, K, L, M, N, O, P, Q, R, S, T, U, V, W, X, a, b, c, d, e, f, g, h
Title Crystal Structure Analysis of Fab1-Bound Human Insulin Degrading Enzyme (IDE) in Complex with Insulin
Classification HYDROLASE
Compound Insulin-degrading enzyme
Source (5WOB)
Sequence A:  NPAIKRIGNHITKSPEDKREYRGLELANGIKVLLISDPTT
DKSSAALDVHIGSLSDPPNIAGLSHFLQHMLFLGTKKYPK
ENEYSQFLSEHAGSSNAFTSGEHTNYYFDVSHEHLEGALD
RFAQFFLFDESAKDREVNAVDSEHEKNVMNDAWRLFQLEK
ATGNPKHPFSKFGTGNKYTLETRPNQEGIDVRQELLKFHA
YYSSNLMAVVVLGRESLDDLTNLVVKLFSEVENKNVPLPE
FPEHPFQEEHLKQLYKIVPIKDIRNLYVTFPIPDLQKYYK
SNPGHYLGHLIGHEGPGSLLSELKSKGWVNTLVGGQKEGA
RGFMFFIINVDLTEEGLLHVEDIILHMFQYIQKLRAEGPQ
EWVFQELKDLNAVAFRFKDKERPRGYTSKIAGILHYYPLE
EVLTAEYLLEEFRPDLIEMVLDKLRPENVRVAIVSKSFEG
KTDRTEEWYGTQYKQEAIPDEVIKKWQNADLNGKFKLPTK
NEFIPTNFEILPLEKEATPYPALIKDTAMSKLWFKQDDKF
FLPKANLNFEFFSPFAYVDPLHSNMAYLYLELLKDSLNEY
AYAAELAGLSYDLQNTIYGMYLSVKGYNDKQPILLKKIIE
KMATFEIDEKRFEIIKEAYMRSLNNFRAEQPHQHAMYYLR
LLMTEVAWTKDELKEALDDVTLPRLKAFIPQLLSRLHIEA
LLHGNITKQAALGIMQMVEDTLIEHAHTKPLLPSQLVRYR
EVQLPDRGWFVYQQRNEVHNNSGIEIYYQTDMQSTSENMF
LELFAQIISEPAFNTLRTKEQLGYIVFSGPRRANGIQGLR
FIIQSEKPPHYLESRVEAFLITMEKSIEDMTEEAFQKHIQ
ALAIRRLDKPKKLSAESAKYWGEIISQQYNFDRDNTEVAY
LKTLTKDIIKFYKEMLVDAPRRHKVSVHVLAQAPALPQPE
VIQNMTEFKRGLPLFPLVKPH
B:  PAIKRIGNHITKSPEDKREYRGLELANGIKVLLISDPTTD
KSSAALDVHIGSLSDPPNAGLSHFLQHMLFLKKYPKENEY
SQFLSEHAGSSNAFTSGEHTNYYFDVSHEHLEGALDRFAQ
FFPLFDESAKDREVNAVDSEHEKNVMNDAWRLFQLEKATG
NPKHPFSKFGTGNKYTLETRPNQEGIDVRQELLKFHSAYY
SSNLMAVVVLGRESLDDLTNLVVKLFSEVENKNVPLPEFP
EHPFQEEHLKQLYKIVPIKDIRNLYVTFPIPDLQKYYKSN
PGHYLGHLIGHEGPGSLLSELKSKGWVNTLVGGQKEGARG
FMFFIINVDLTEEGLLHVEDIILHMFQYIQKLRAEGPQEW
VFQELKDLNAVAFRFKDKERPRGYTSKIAGILHYYPLEEV
LTAEYLLEEFRPDLIEMVLDKLRPENVRVAIVSKSFEGKT
DRTEEWYGTQYKQEAIPDEVIKKWQNADLNGKFKLPTKNE
FIPTNFEILPLEKETPYPALIKDTAMSKLWFKQDDKFFLP
KANLNFEFFSPFAYVDPLHSNMAYLYLELLKDSLNEYAYA
AELAGLSYDLQNTIYGMYLSVKGYNDKQPILLKKIIEKMA
TFEIDEKRFEIIKEAYMRSLNNFRAEQPHQHAMYYLRLLM
TEVAWTKDELKEALDDVTLPRLKAFIPQLLSRLHIEALLH
GNITKQAALGIMQMVEDTLIEHAHTKPLLPSQLVRYREVQ
LPDRGWFVYQQRNEVHNNSGIEIYYQTDMQSTSENMFLEL
FAQIISEPAFNTLRTKEQLGYIVFSGPRRANGIQGLRFII
QSEKPPHYLESRVEAFLITMEKSIEDMTEEAFQKHIQALA
IRRLDKPKKLSAESAKYWGEIISQQYNFDRDNTEVAYLKT
LTKEDIIKFYKEMLAVDAPRRHKVSVHVLAREMDSNNLSQ
APALPQPEVIQNMTEFKRGLPLFPLVK
C:  NPAIKRIGNHITKSPEDKREYRGLELANGIKVLLISDPTT
DKSSAALDVHIGSLSDPPNIAGLSHFLQHMLFLGTKKYPK
ENEYSQFLSEHAGSSNAFTSGEHTNYYFDVSHEHLEGALD
RFAQFFLSPLFDESAKDREVNAVDSEHEKNVMNDAWRLFQ
LEKATGNPKHPFSKFGTGNKYTLETRPNQEGIDVRQELLK
FHSAYYSSNLMAVVVLGRESLDDLTNLVVKLFSEVENKNV
PLPEFPEHPFQEEHLKQLYKIVPIKDIRNLYVTFPIPDLQ
KYYKSNPGHYLGHLIGHEGPGSLLSELKSKGWVNTLVGGQ
KEGARGFMFFIINVDLTEEGLLHVEDIILHMFQYIQKLRA
EGPQEWVFQELKDLNAVAFRFKDKERPRGYTSIAGILHYY
PLEEVLTAEYLLEEFRPDLIEMVLDKLRPENVRVAIVSKS
FEGKTDRTEEWYGTQYKQEAIPDEVIKKWQNADLNGKFKL
PTKNEFIPTNFEILPLEKEATPYPALIKDTAMSKLWFKQD
DKFFLPKANLNFEFFSPFAYVDPLHSNMAYLYLELLKDSL
NEYAYAAELAGLSYDLQNTIYGMYLSVKGYNDKQPILLKK
IIEKMATFEIDEKRFEIIKEAYMRSLNNFRAEQPHQHAMY
YLRLLMTEVAWTKDELKEALDDVTLPRLKAFIPQLLSRLH
IEALLHGNITKQAALGIMQMVEDTLIEHAHTKPLLPSQLV
RYREVQLPDRGWFVYQQRNEVHNNSGIEIYYQTDMQSTSE
NMFLELFAQIISEPAFNTLRTKEQLGYIVFSGPRRANGIQ
GLRFIIQSEKPPHYLESRVEAFLITMEKSIEDMTEEAFQK
HIQALAIRRLDKPKKLSAESAKYWGEIISQQYNFDRDNTE
VAYLKTLTKDIIKFYKEMLAVDAPRRHKVSVHVLAREMDS
APALPQPEVIQNMTEFKRGLPLFPLVKPHI
D:  NPAIKRIGNHITKSPEDKREYRGLELANGIKVLLISDPTT
DKSSAALDVHIGSLSDPPNIAGLSHFLQHMLFLGTKKYPK
ENEYSQFLSEHAGSSNAFTSGEHTNYYFDVSHEHLEGALD
RFAQFFLSPLFDESAKDREVNAVDSEHEKNVMNDAWRLFQ
LEKATGNPKHPFSKFGTGNKYTLETRPNQEGIDVRQELLK
FHSAYYSNLMAVVVLGRESLDDLTNLVVKLFSEVENKNVP
LPEFPEHPFQEEHLKQLYKIVPIKDIRNLYVTFPIPDLQK
YYKSNPGHYLGHLIGHEGPGSLLSELKSKGWVNTLVGGQK
EGARGFMFFIINVDLTEEGLLHVEDIILHMFQYIQKLRAE
GPQEWVFQELKDLNAVAFRFKDKERPRGYTSKIAGILHYY
PLEEVLTAEYLLEEFRPDLIEMVLDKLRPENVRVAIVSKS
FEGKTDRTEEWYGTQYKQEAIPDEVIKKWQNADLNGKFKL
PTKNEFIPTNFEILPLEKEATPYPALIKDTAMSKLWFKQD
DKFFLPKANLNFEFFSPFAYVDPLHSNMAYLYLELLKDSL
NEYAYAAELAGLSYDLQNTIYGMYLSVKGYNDKQPILLKK
IIEKMATFEIDEKRFEIIKEAYMRSLNNFRAEQPHQHAMY
YLRLLMTEVAWTKDELKEALDDVTLPRLKAFIPQLLSRLH
IEALLHGNITKQAALGIMQMVEDTLIEHAHTKPLLPSQLV
RYREVQLPDRGWFVYQQRNEVHNNSGIEIYYQTDMQSTSE
NMFLELFAQIISEPAFNTLRTKEQLGYIVFSGPRRANGIQ
GLRFIIQSEKPPHYLESRVEAFLITMEIEDMTEEAFQKHI
QALAIRRLDKPKKLSAESAKYWGEIISQQYNFDRDNTEVA
YLKTLTKEDIIKFYKEMLAVDAPRRHKVSVHVLAREMDSN
NLSQAPALPQPEVIQNMTEFKRGLPLFPLVKP
E:  NPAIKRIGNHITKSPEDKREYRGLELANGIKVLLISDPTT
DKSSAALDVHIGSLSDPPNIAGLSHFLQHMLFLKKYPKEN
EYQFLSEHAGSSNAFTSGEHTNYYFDVSHEHLEGALDRFA
FFSPFDSAKDREVNAVDSEHEKNVMNDAWRLFQLEKATGN
PKHPFSKFGTGNKYTLTRPNQEGIDVRQELLKFHSAYYSS
NLMAVVVLGRESLDDLTNLVVKLFSEVENKNVPLPEFPEH
PFQEEHLKQLYKIVPIKDIRNLYVTFPIPDLQKYYKSNPG
HYLGHLIGHEGPGSLLSELKSKGWVNTLVGGQKEGARGFM
FFIINVDLTEEGLLHVEDIILHMFQYIQKLRAEGPQEWVF
QELKDLNAVAFRFKDKERPRGYTSKIAGILHYYPLEEVLT
AEYLLEEPDLIEMVLDKLRPENVRVAIVSKSFEGKTDRTE
EWYGTQYKQEAIPDEVIKKWQNADLNGKFKLPTKNEFIPT
NFEILPLEKEATPYPALIKDTAMSKLWFKQDDKFFLPKAN
LNFEFFSPFAYVDPLHSNMAYLYLELLKDSLNEYAYAAEL
AGLSYDLQNTIYGMYLSVKGYNDKQPILLKKIIEKMATFE
IDEKRFEIIKEAYMRSLNNFRAEQPHQHAMYYLRLLMTEV
AWTKDELKEALDDVTLPRLKAFIPQLLSRLHIEALLHGNI
TKQAALGIMQMVEDTLIEHAHTKPLLPSQLVRYREVQLPD
RGWFVYQQRNEVHNNSGIEIYYQTDMQSTSENMFLELFAQ
IISEPAFNTLRTKEQLGYIVFSGPRRANGIQGLRFIIQSE
KPPHYLESRVEAFLITMEKSIEDMTEEAFQKHIQALAIRR
LDKPKKLSAESAKYWGEIISQQYNFDRDNTEVAYLKTLTK
EDIIKFYKEMLAVDAPRRHKVSVHVLAREMDSNSQAPALP
QPEVIQNMTEFKRGLPLFPLVKP
F:  NPAIKRIGNHITKSPEDKREYRGLELANGIKVLLISDPTT
DKSSAALDVHIGSLSDPPNIAGLSHFLQHMLFLGTKKYPK
ENEYSQFLSEHAGSSNAFTSGEHTNYYFDVSHEHLEGALD
RFAQFFLSPLFDEKDREVNAVDSEHEKNVMNDAWRLFQLE
KATGNPKHPFSKFGTGNKYTLTRPNQEGIDVRQELLKFHS
AYYSSNLMAVVVLGRESLDDLTNLVVKLFSEVENKNVPLP
EFPEHPFQEEHLKQLYKIVPIKDIRNLYVTFPIPDLQKYY
KSNPGHYLGHLIGHEGPGSLLSELKSKGWVNTLVGGQKEG
ARGFMFFIINVDLTEEGLLHVEDIILHMFQYIQKLRAEGP
QEWVFQELKDLNAVAFRFKDKERPRGYTSKIAGILHYYPL
EEVLTAEYLLEEFRPDLIEMVLDKLRPENVRVAIVSKSFE
GKTDRTEEWYGTQYKQEAIPDEVIKKWQNADLNGKFKLPT
KNEFIPTNFEILPLEKEATPYPALIKDTAMSKLWFKQDDK
FLPKANLNFEFFSPFAYVDPLHSNMAYLYLELLKDSLNEY
AYAAELAGLSYDLQNTIYGMYLSVKGYNDKQPILLKKIIE
KMATFEIDEKRFEIIKEAYMRSLNNFRAEQPHQHAMYYLR
LLMTEVAWTKDELKEALDDVTLPRLKAFIPQLLSRLHIEA
LLHGNITKQAALGIMQMVEDTLIEHAHTKPLLPSQLVRYR
EVQLPDRGWFVYQQRNEVHNNGIEIYYQTDMQSTSENMFL
ELFAQIISEPAFNTLRTKEQLGYIVFSGPRRANGIQGLRF
IIQSEKPPHYLESRVEAFLITMEKSIETEFQKHIQALAIR
RLDKPKKLSAESAKYWGEIISQQYNFDRDNTEVAYLKTLT
KEDIIKFYKEMLAVDPRRHKVSVHVLAREMINLSQAPALP
QPEVIQNMTEFKRGLPLFPLVKPH
G:  NPAIKRIGNHITKSPEDKREYRGLELANGIKVLLISDPTT
DKSSAALDVHIGSLSDPPNIAGLSHFLQHMLFLKKYPKEN
EYQFLSEHAGSSNAFTSGEHTNYYFDVSHEHLEGALDRFA
QFFLSFDESAKDREVNAVDSHEKNVMNAWRLFQLEKATGN
PKHPFSKFTGNKYTLTRPNQEGIDVRQELLKFHSAYYSSN
LMAVVVLGRESLDDLTNLVVKLFSEVENKNVPLPEFPEHP
FQEEHLKQLYKIVPIKDIRNLYVTFPIPDLQKYYKSNPGH
YLGHLIGHEGPGSLLSELKSKGWVNTLVGGQKEGARGFMF
FIINVDLTEEGLLHVEDIILHMFQYIQKLRAEGPQEWVFQ
ELKDLNAVAFRFKDKERPRGYTSKIAGILHYYPLEEVLTA
EYLLEEFRPDLIEMVLDKLRPENVRVAIVSKSFEGKTDRT
EEWYGTQYKQEAIPDEVIKKWQNADLNGKFKLPTKNEFIP
TNFEILPLEKEATPYPALIKDTAMSKLWFKQDDKFFLPKA
NLNFEFFSPFAYVDPLHSNMAYLYLELLKDSLNEYAYAAE
LAGLSYDLQNTIYGMYLSVKGYNDKQPILLKKIIEKMATF
EIDEKRFEIIKEAYMRSLNNFRAEQPHQHAMYYLRLLMTE
VAWTKDELKEALDDVTLPRLKAFIPQLLSRLHIEALLHGN
ITKQAALGIMQMVEDTLIEHAHTKPLLPSQLVRYREVQLP
DRGWFVYQQRNEVHNNSGIEIYYQTDMQSTSENMFLELFA
QIISEPAFNTLRTKEQLGYIVFSGPRRANGIQGLRFIIQS
EKPPHYLESRVEAFLITMEKSIEDMTEEAQKHIQALAIRR
LDKPKKLSAESAKYWGEIISQQYNFDRDNTEVAYLKTLTK
EDIIKFYKEMLAVDAPRRHKVSVHVLAREMDSNSQAPALP
QPEVIQNMTEFKRGLPLFPLVKP
H:  NPAIKRIGNHITKSPEDKREYRGLELANGIKVLLISDPTT
DKSSAALDVHIGSLSDPPNAGLSHFLQHMLFLGTKKYPNE
YSQFLSEHAGSSNAFTSGEHTNYYFDVSHEHLEGALDRFA
QFFLSPLFDEAKDREVNAVDSEHEKNVMNDAWRLFQLEKA
TGNPKHPFSKFGTGNKYTLETRPNQEGIDVRQELLKFHSA
YYSSNLMAVVVLGRESLDDLTNLVVKLFSEVENKNVPLPE
FPEHPFQEEHLKQLYKIVPIKDIRNLYVTFPIPDLQKYYK
SNPGHYLGHLIGHEGPGSLLSELKSKGWVNTLVGGQKEGA
RGFMFFIINVDLTEEGLLHVEDIILHMFQYIQKLRAEGPQ
EWVFQELKDLNAVAFRFKDKERPRGYTSKIAGILHYYPLE
EVLTAEYLLEEFRPDLIEMVLDKLRPENVRVAIVSKSFEG
KTDRTEEWYGTQYKQEAIPDEVIKKWQNADLNGKFKLPTK
NEFIPTNFEILPLEKEATPYPALIKDTAMSKLWFKQDDKF
FLPKANLNFEFFSPFAYVDPLHSNMAYLYLELLKDSLNEY
AYAAELAGLSYDLQNTIYGMYLSVKGYNDKQPILLKKIIE
KMATFEIDEKRFEIIKEAYMRSLNNFRAEQPHQHAMYYLR
LLMTEVAWTKDELKEALDDVTLPRLKAFIPQLLSRLHIEA
LLHGNITKQAALGIMQMVEDTLIEHAHTKPLLPSQLVRYR
EVQLPDRGWFVYQQRNEVHNNSGIEIYYQTDMQSTSENMF
LELFAQIISEPAFNTLRTKEQLGYIVFSGPRRANGIQGLR
FIIQSEKPPHYLESRVEAFLITMEKSIEFQKHIQALAIRR
LDKPKKLSAESAKYWGEIISQQYNFDRDNTEVAYLKTLTK
EDIIKFYKEMLAVDAPRRHKVSVHVLARAPALPQPEVIQN
MTEFKRGLPLFPLVKP
I:  EVQLVESGGGLVQPGGSLRLSCAASGFNVSSYSIHWVRQA
PGKGLEWVASISSYYGSTSYADSVKGRFTISADTNTAYLQ
MNSLRAEDTAVYYCARDRVMYYWSFSKYGYPYGMDYWGQG
TLVTVSSASTKGPSVFPLAPTAALGCLVKDYFPEPVTVSW
NSGALTSGVHTFPAVLQSSGLYSLSSVVTVPSSTYICNVN
HKPSNTKVDKKVEPK
J:  MTQSPSSLSASVGDRVTITCRAVSSAVAWYQQKPGKAPKL
LIYSTSSLYSGVPSRFSGSRSTDFTLTISSLQPEDFATYY
CQQSSPSFLITFGQGTKVEIKRTVAAPSVFIFPPSDSQLK
SASVVCLLNNFYPREAKVQWKALSGNSQESVTEQDSKDST
YSLSSTLTLSKADYEKHKVYCEVTHQGLSSPVTKSFNR
K:  EVQLVESGGGLVQPGGSLRLSCAASGFNVSSYSIHWVRQA
PGKGLEWVASISSYYGSTSYADSVKGRFTISADTNTAYLQ
MNSLRAEDAVYYCARDRVMYYWSFSKYGYPYGMDYWGQGT
LVTVSSASTKGPSVFPLAPSSGCLVKDYFPEPVTVSWNSG
VHTFPAVLQSSGLYSLSSVVTVPSSTYICNVNHKPSNTKV
DKKVEPK
L:  MTQSPSSLSASVGDRVTITCRAVSSAVAWYQQKPGKAPKL
LIYSTSSLYSGVPSRFSGSRSTDFTLTISSLQPEDFATYY
CQQSSPSFLITFGQGTKVEIKRVAAPSVFIFPPSDSQLKS
SVVCLLNNFYPREAKVQWKSGNSQESVTEQDSKDSTYSLS
STLTYEKHKVTHQGLS
M:  EVQLVESGGGLVQPGGSLRLSCAASGFNVSSYSIHWVRQA
PGKGLEWVASISSYYGSTSYADSVKGRFTISADTNTAYLQ
MNSLRAEDTAVYYCARDRVMYYWSFSKYGYPYGMDYWGQG
TLVTVSSASTKGPSVFPLAPTAALGCLVKDYFPEPVTVSW
NSGALTSGVHTFPAVLQSSGLYSLSSVVTVPSSTYICNVN
HKPSNTKVDKKVEP
N:  MTQSPSSLSASVGDRVTITCRAVSSAVAWYQQKPGKAPKL
LIYSTSSLYSGVPSRFSGSRSGTDFTLTISSLQPEDFATY
YCQQSSPSFLITFGQGTKVEIKRTVAAPSVFIFPPSDSQL
KSASVVCLLNNFYPREAKVQWKALSGNSQESVTEQDSKDS
TYSLSSTLTLSKADYEKHKVYACEVTHQGLSSPVTKSFNR
O:  EVQLVESGGGLVQPGGSLRLSCAASGFNVSSYSIHWVRQA
PGKGLEWVASISSYYGSTSYADSVKGRFTISADTNTAYLQ
MNSLRAEDTAVYYCARDRVMYYWSFSKYGYPYGMDYWGQG
TLVTVSSASTKGPSVFPLAPSSLGCLVKDYFPEPVTVSWN
SGALSGVHTFPAVLQSSGLYSLSSVVTVPSSNVNHKPSNT
KVDKKVEPK
P:  MTQSPSSLSASVGDRVTITCRAVSSAVAWYQQKPGKAPKL
LIYSTSSLYSGVPSRFSGSRSGTDFTLTISSLQPEDFATY
YCQQSSPSFLITFGQGTKVEIKRTVAAPSVFIFPPSDSQL
KASVVCLLNNFYPREAKVQWKALSGNSQESVTEQDSKDST
YSLSSTLYEKHKCVTHQGTKSFNR
Q:  EVQLVESGGGLVQPGSLRLSCAASGFNVSSYSIHWVRQAP
GKGLEWVASISSYYGSTYADSVKGRFTISADTNTAYLQSL
RAEDAVYYCARDRVMYYWSFSKYGYPYGMDYWGQGTLVTV
SSASTKGPSVFPLAPSSGCLVKDYFPEPVTVSWNSGALSG
VHTFPAVLQSSGLYSLSSVVTYICNVNHKSNTKVDKKVEP
K
R:  MTQSPSSLSASVGDRVTITCRAVSSAVAWYQQKPGKAPKL
LIYSTSSLYSGVPSRFSGSRSGTDFTLTISSLQPEDFATY
YCQQSSPSFLITFGQGTKVEIKRTVAAPSVFIFPPSDSQL
KSVCLLNNFYPREASGNSQESVTEQDSKDSTYSLSSTLSK
ADYEKHKVYATHQGLSS
S:  EVQLVESGGGLVQPGGSLRLSCAASGFNVSSYSIHWVRQA
PGKGLEWVASISSYYGSTSYADSVKGRFTISADTNTAYLQ
MNSLRAEDTAVYYCARDRVMYYWSFSKYGYPYGMDYWGQG
TLVTVSSASTKGPSVFPLAPTAALGCLVKDYFPEPVTVSW
NSGALTSGVHTFPAVLQSSGLYSLSSVVTVPSSTYICNVN
HKPSNTKVDKKVEPK
T:  MTQSPSSLSASVGDRVTITCRASQSVSSAVAWYQQKPGKA
PKLLIYSTSSLYSGVPSRFSGSRSTDFTLTISSLQPEDFA
TYYCQQSSPSFLITFGQGTKVEIKRTVAAPSVFIFPPSDS
QLKSASVVCLLNNFYPREAKVQWKSGNSQESVTEQDSKDS
TYSLSSTLTLSKADYEKHKVACEVTHQGLSSPVTKFNR
U:  EVQLVESGGGLVQPGGSLRLSCAASGFNVSSYSIHWVRQA
PGKGLEWVASISSYYGSTSYADSVKGRFTISADTNTAYLQ
MNSLRAEDTAVYYCARDRVMYYWSFSKYGYPYGMDYWGQG
ASTKGPSVFPLATAALGCLVDYFPEPVTVSWSGALTSGVH
TFPAVLQSSGLYSSVVTVPTYICNVNHKPSNTKVDKKVE
V:  MTQSPSSLSASVGDRVTITCRAVSSAVAWYQQKPGKAPKL
LIYSTSSLYSGVPSRFSGSRSGTDFTLTISLQPEDFATYY
CQQSSPSFLITFGQGTKVEIKRTVAAPSVFIFPPDSQLKS
NFYPREAKVQWALSGNSQESVTEQDSKDSTYSLSSTLTSK
ADYEKHYACEVTHQGLSSPVTKSFNR
W:  EVQLVESGGGLVQPGGSLRLSCAASGFNVSSYSIHWVRQA
PGKGLEWVASISSYYGSTSYADSVKGRFTISADTNTAYLQ
MNSLRAEDTAVYYCARDRVMYYWSFSKYGYPYGMDYWGQG
TLVTVSSGPSVFPLAPSSTAALGLVKDYFPEPVTVSWNSG
ALTSGVHTFPAVLQSSGLYSLSSVVTVPSSTYICNVNHKP
SNTK
X:  TQSPSSLSASVGDRVTITCRASQSVSSAVAWYQQKPGKAP
KLLIYSTSSLYSGVPSRFSGSRSGTDFTLTISSLQPEDFA
TYYCQQSSPSFLITFGQGTKVEIKRTVAAPSVFIFPPSDS
QLKSASVVCLLNNFYPREAKVQWKSGNSQESVTEQDSKDS
TYSLSSTLTLSKADYEKHKVCEVTHQGLSSPVTKSFNR
a:  GIVEQCCTSICSLYQLENYC
b:  GIVEQ
c:  GIVEQCCTSICSLYQLENYC
d:  GIV
e:  GIVEQLYQL
f:  GIVEQCCTSICSQLENYC
g:  GIVEQCSLYQLENYC
h:  GIVEQC
Description


Functional site

1) chain A
residue 108
type
sequence H
description binding site for residue ZN A 1101
source : AC1

2) chain A
residue 112
type
sequence H
description binding site for residue ZN A 1101
source : AC1

3) chain A
residue 189
type
sequence E
description binding site for residue ZN A 1101
source : AC1

4) chain a
residue 12
type
sequence S
description binding site for residue ZN A 1101
source : AC1

5) chain a
residue 14
type
sequence Y
description binding site for residue ZN A 1101
source : AC1

6) chain B
residue 108
type
sequence H
description binding site for residue ZN B 2001
source : AC2

7) chain B
residue 112
type
sequence H
description binding site for residue ZN B 2001
source : AC2

8) chain B
residue 189
type
sequence E
description binding site for residue ZN B 2001
source : AC2

9) chain C
residue 108
type
sequence H
description binding site for residue ZN C 1101
source : AC3

10) chain C
residue 112
type
sequence H
description binding site for residue ZN C 1101
source : AC3

11) chain C
residue 189
type
sequence E
description binding site for residue ZN C 1101
source : AC3

12) chain c
residue 14
type
sequence Y
description binding site for residue ZN C 1101
source : AC3

13) chain D
residue 108
type
sequence H
description binding site for residue ZN D 2001
source : AC4

14) chain D
residue 112
type
sequence H
description binding site for residue ZN D 2001
source : AC4

15) chain D
residue 189
type
sequence E
description binding site for residue ZN D 2001
source : AC4

16) chain E
residue 108
type
sequence H
description binding site for residue ZN E 2001
source : AC5

17) chain E
residue 112
type
sequence H
description binding site for residue ZN E 2001
source : AC5

18) chain E
residue 189
type
sequence E
description binding site for residue ZN E 2001
source : AC5

19) chain F
residue 108
type
sequence H
description binding site for residue ZN F 1101
source : AC6

20) chain F
residue 112
type
sequence H
description binding site for residue ZN F 1101
source : AC6

21) chain F
residue 189
type
sequence E
description binding site for residue ZN F 1101
source : AC6

22) chain G
residue 108
type
sequence H
description binding site for residue ZN G 2001
source : AC7

23) chain G
residue 112
type
sequence H
description binding site for residue ZN G 2001
source : AC7

24) chain H
residue 108
type
sequence H
description binding site for residue ZN H 1101
source : AC8

25) chain H
residue 112
type
sequence H
description binding site for residue ZN H 1101
source : AC8

26) chain H
residue 189
type
sequence E
description binding site for residue ZN H 1101
source : AC8

27) chain a
residue 6-20
type prosite
sequence CCTSICSLYQLENYC
description INSULIN Insulin family signature. CCTSiCSlyqLenyC
source prosite : PS00262

28) chain I
residue 210-216
type prosite
sequence YICNVNH
description IG_MHC Immunoglobulins and major histocompatibility complex proteins signature. YACEVTH
source prosite : PS00290

29) chain N
residue 193-199
type prosite
sequence YACEVTH
description IG_MHC Immunoglobulins and major histocompatibility complex proteins signature. YACEVTH
source prosite : PS00290

30) chain A
residue 192
type MOD_RES
sequence K
description N6-succinyllysine => ECO:0000250|UniProtKB:Q9JHR7
source Swiss-Prot : SWS_FT_FI6

31) chain E
residue 697
type MOD_RES
sequence K
description N6-succinyllysine => ECO:0000250|UniProtKB:Q9JHR7
source Swiss-Prot : SWS_FT_FI6

32) chain F
residue 192
type MOD_RES
sequence K
description N6-succinyllysine => ECO:0000250|UniProtKB:Q9JHR7
source Swiss-Prot : SWS_FT_FI6

33) chain F
residue 697
type MOD_RES
sequence K
description N6-succinyllysine => ECO:0000250|UniProtKB:Q9JHR7
source Swiss-Prot : SWS_FT_FI6

34) chain G
residue 192
type MOD_RES
sequence K
description N6-succinyllysine => ECO:0000250|UniProtKB:Q9JHR7
source Swiss-Prot : SWS_FT_FI6

35) chain G
residue 697
type MOD_RES
sequence K
description N6-succinyllysine => ECO:0000250|UniProtKB:Q9JHR7
source Swiss-Prot : SWS_FT_FI6

36) chain H
residue 192
type MOD_RES
sequence K
description N6-succinyllysine => ECO:0000250|UniProtKB:Q9JHR7
source Swiss-Prot : SWS_FT_FI6

37) chain H
residue 697
type MOD_RES
sequence K
description N6-succinyllysine => ECO:0000250|UniProtKB:Q9JHR7
source Swiss-Prot : SWS_FT_FI6

38) chain A
residue 697
type MOD_RES
sequence K
description N6-succinyllysine => ECO:0000250|UniProtKB:Q9JHR7
source Swiss-Prot : SWS_FT_FI6

39) chain B
residue 192
type MOD_RES
sequence K
description N6-succinyllysine => ECO:0000250|UniProtKB:Q9JHR7
source Swiss-Prot : SWS_FT_FI6

40) chain B
residue 697
type MOD_RES
sequence K
description N6-succinyllysine => ECO:0000250|UniProtKB:Q9JHR7
source Swiss-Prot : SWS_FT_FI6

41) chain C
residue 192
type MOD_RES
sequence K
description N6-succinyllysine => ECO:0000250|UniProtKB:Q9JHR7
source Swiss-Prot : SWS_FT_FI6

42) chain C
residue 697
type MOD_RES
sequence K
description N6-succinyllysine => ECO:0000250|UniProtKB:Q9JHR7
source Swiss-Prot : SWS_FT_FI6

43) chain D
residue 192
type MOD_RES
sequence K
description N6-succinyllysine => ECO:0000250|UniProtKB:Q9JHR7
source Swiss-Prot : SWS_FT_FI6

44) chain D
residue 697
type MOD_RES
sequence K
description N6-succinyllysine => ECO:0000250|UniProtKB:Q9JHR7
source Swiss-Prot : SWS_FT_FI6

45) chain E
residue 192
type MOD_RES
sequence K
description N6-succinyllysine => ECO:0000250|UniProtKB:Q9JHR7
source Swiss-Prot : SWS_FT_FI6

46) chain A
residue 111
type ACT_SITE
sequence Q
description Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU10096, ECO:0000305|PubMed:10684867, ECO:0000305|PubMed:17051221, ECO:0000305|PubMed:19321446, ECO:0000305|PubMed:23922390
source Swiss-Prot : SWS_FT_FI1

47) chain B
residue 111
type ACT_SITE
sequence Q
description Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU10096, ECO:0000305|PubMed:10684867, ECO:0000305|PubMed:17051221, ECO:0000305|PubMed:19321446, ECO:0000305|PubMed:23922390
source Swiss-Prot : SWS_FT_FI1

48) chain C
residue 111
type ACT_SITE
sequence Q
description Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU10096, ECO:0000305|PubMed:10684867, ECO:0000305|PubMed:17051221, ECO:0000305|PubMed:19321446, ECO:0000305|PubMed:23922390
source Swiss-Prot : SWS_FT_FI1

49) chain D
residue 111
type ACT_SITE
sequence Q
description Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU10096, ECO:0000305|PubMed:10684867, ECO:0000305|PubMed:17051221, ECO:0000305|PubMed:19321446, ECO:0000305|PubMed:23922390
source Swiss-Prot : SWS_FT_FI1

50) chain E
residue 111
type ACT_SITE
sequence Q
description Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU10096, ECO:0000305|PubMed:10684867, ECO:0000305|PubMed:17051221, ECO:0000305|PubMed:19321446, ECO:0000305|PubMed:23922390
source Swiss-Prot : SWS_FT_FI1

51) chain F
residue 111
type ACT_SITE
sequence Q
description Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU10096, ECO:0000305|PubMed:10684867, ECO:0000305|PubMed:17051221, ECO:0000305|PubMed:19321446, ECO:0000305|PubMed:23922390
source Swiss-Prot : SWS_FT_FI1

52) chain G
residue 111
type ACT_SITE
sequence Q
description Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU10096, ECO:0000305|PubMed:10684867, ECO:0000305|PubMed:17051221, ECO:0000305|PubMed:19321446, ECO:0000305|PubMed:23922390
source Swiss-Prot : SWS_FT_FI1

53) chain H
residue 111
type ACT_SITE
sequence Q
description Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU10096, ECO:0000305|PubMed:10684867, ECO:0000305|PubMed:17051221, ECO:0000305|PubMed:19321446, ECO:0000305|PubMed:23922390
source Swiss-Prot : SWS_FT_FI1

54) chain D
residue 108
type BINDING
sequence H
description BINDING => ECO:0000255|PROSITE-ProRule:PRU10096, ECO:0000269|PubMed:17051221, ECO:0000269|PubMed:17613531, ECO:0000269|PubMed:18986166, ECO:0000269|PubMed:19321446, ECO:0007744|PDB:2G54, ECO:0007744|PDB:2JG4, ECO:0007744|PDB:3CWW, ECO:0007744|PDB:3N56, ECO:0007744|PDB:3N57
source Swiss-Prot : SWS_FT_FI2

55) chain D
residue 112
type BINDING
sequence H
description BINDING => ECO:0000255|PROSITE-ProRule:PRU10096, ECO:0000269|PubMed:17051221, ECO:0000269|PubMed:17613531, ECO:0000269|PubMed:18986166, ECO:0000269|PubMed:19321446, ECO:0007744|PDB:2G54, ECO:0007744|PDB:2JG4, ECO:0007744|PDB:3CWW, ECO:0007744|PDB:3N56, ECO:0007744|PDB:3N57
source Swiss-Prot : SWS_FT_FI2

56) chain D
residue 189
type BINDING
sequence E
description BINDING => ECO:0000255|PROSITE-ProRule:PRU10096, ECO:0000269|PubMed:17051221, ECO:0000269|PubMed:17613531, ECO:0000269|PubMed:18986166, ECO:0000269|PubMed:19321446, ECO:0007744|PDB:2G54, ECO:0007744|PDB:2JG4, ECO:0007744|PDB:3CWW, ECO:0007744|PDB:3N56, ECO:0007744|PDB:3N57
source Swiss-Prot : SWS_FT_FI2

57) chain E
residue 108
type BINDING
sequence H
description BINDING => ECO:0000255|PROSITE-ProRule:PRU10096, ECO:0000269|PubMed:17051221, ECO:0000269|PubMed:17613531, ECO:0000269|PubMed:18986166, ECO:0000269|PubMed:19321446, ECO:0007744|PDB:2G54, ECO:0007744|PDB:2JG4, ECO:0007744|PDB:3CWW, ECO:0007744|PDB:3N56, ECO:0007744|PDB:3N57
source Swiss-Prot : SWS_FT_FI2

58) chain E
residue 112
type BINDING
sequence H
description BINDING => ECO:0000255|PROSITE-ProRule:PRU10096, ECO:0000269|PubMed:17051221, ECO:0000269|PubMed:17613531, ECO:0000269|PubMed:18986166, ECO:0000269|PubMed:19321446, ECO:0007744|PDB:2G54, ECO:0007744|PDB:2JG4, ECO:0007744|PDB:3CWW, ECO:0007744|PDB:3N56, ECO:0007744|PDB:3N57
source Swiss-Prot : SWS_FT_FI2

59) chain E
residue 189
type BINDING
sequence E
description BINDING => ECO:0000255|PROSITE-ProRule:PRU10096, ECO:0000269|PubMed:17051221, ECO:0000269|PubMed:17613531, ECO:0000269|PubMed:18986166, ECO:0000269|PubMed:19321446, ECO:0007744|PDB:2G54, ECO:0007744|PDB:2JG4, ECO:0007744|PDB:3CWW, ECO:0007744|PDB:3N56, ECO:0007744|PDB:3N57
source Swiss-Prot : SWS_FT_FI2

60) chain F
residue 108
type BINDING
sequence H
description BINDING => ECO:0000255|PROSITE-ProRule:PRU10096, ECO:0000269|PubMed:17051221, ECO:0000269|PubMed:17613531, ECO:0000269|PubMed:18986166, ECO:0000269|PubMed:19321446, ECO:0007744|PDB:2G54, ECO:0007744|PDB:2JG4, ECO:0007744|PDB:3CWW, ECO:0007744|PDB:3N56, ECO:0007744|PDB:3N57
source Swiss-Prot : SWS_FT_FI2

61) chain F
residue 112
type BINDING
sequence H
description BINDING => ECO:0000255|PROSITE-ProRule:PRU10096, ECO:0000269|PubMed:17051221, ECO:0000269|PubMed:17613531, ECO:0000269|PubMed:18986166, ECO:0000269|PubMed:19321446, ECO:0007744|PDB:2G54, ECO:0007744|PDB:2JG4, ECO:0007744|PDB:3CWW, ECO:0007744|PDB:3N56, ECO:0007744|PDB:3N57
source Swiss-Prot : SWS_FT_FI2

62) chain F
residue 189
type BINDING
sequence E
description BINDING => ECO:0000255|PROSITE-ProRule:PRU10096, ECO:0000269|PubMed:17051221, ECO:0000269|PubMed:17613531, ECO:0000269|PubMed:18986166, ECO:0000269|PubMed:19321446, ECO:0007744|PDB:2G54, ECO:0007744|PDB:2JG4, ECO:0007744|PDB:3CWW, ECO:0007744|PDB:3N56, ECO:0007744|PDB:3N57
source Swiss-Prot : SWS_FT_FI2

63) chain G
residue 108
type BINDING
sequence H
description BINDING => ECO:0000255|PROSITE-ProRule:PRU10096, ECO:0000269|PubMed:17051221, ECO:0000269|PubMed:17613531, ECO:0000269|PubMed:18986166, ECO:0000269|PubMed:19321446, ECO:0007744|PDB:2G54, ECO:0007744|PDB:2JG4, ECO:0007744|PDB:3CWW, ECO:0007744|PDB:3N56, ECO:0007744|PDB:3N57
source Swiss-Prot : SWS_FT_FI2

64) chain G
residue 112
type BINDING
sequence H
description BINDING => ECO:0000255|PROSITE-ProRule:PRU10096, ECO:0000269|PubMed:17051221, ECO:0000269|PubMed:17613531, ECO:0000269|PubMed:18986166, ECO:0000269|PubMed:19321446, ECO:0007744|PDB:2G54, ECO:0007744|PDB:2JG4, ECO:0007744|PDB:3CWW, ECO:0007744|PDB:3N56, ECO:0007744|PDB:3N57
source Swiss-Prot : SWS_FT_FI2

65) chain H
residue 108
type BINDING
sequence H
description BINDING => ECO:0000255|PROSITE-ProRule:PRU10096, ECO:0000269|PubMed:17051221, ECO:0000269|PubMed:17613531, ECO:0000269|PubMed:18986166, ECO:0000269|PubMed:19321446, ECO:0007744|PDB:2G54, ECO:0007744|PDB:2JG4, ECO:0007744|PDB:3CWW, ECO:0007744|PDB:3N56, ECO:0007744|PDB:3N57
source Swiss-Prot : SWS_FT_FI2

66) chain H
residue 112
type BINDING
sequence H
description BINDING => ECO:0000255|PROSITE-ProRule:PRU10096, ECO:0000269|PubMed:17051221, ECO:0000269|PubMed:17613531, ECO:0000269|PubMed:18986166, ECO:0000269|PubMed:19321446, ECO:0007744|PDB:2G54, ECO:0007744|PDB:2JG4, ECO:0007744|PDB:3CWW, ECO:0007744|PDB:3N56, ECO:0007744|PDB:3N57
source Swiss-Prot : SWS_FT_FI2

67) chain H
residue 189
type BINDING
sequence E
description BINDING => ECO:0000255|PROSITE-ProRule:PRU10096, ECO:0000269|PubMed:17051221, ECO:0000269|PubMed:17613531, ECO:0000269|PubMed:18986166, ECO:0000269|PubMed:19321446, ECO:0007744|PDB:2G54, ECO:0007744|PDB:2JG4, ECO:0007744|PDB:3CWW, ECO:0007744|PDB:3N56, ECO:0007744|PDB:3N57
source Swiss-Prot : SWS_FT_FI2

68) chain C
residue 189
type BINDING
sequence E
description BINDING => ECO:0000255|PROSITE-ProRule:PRU10096, ECO:0000269|PubMed:17051221, ECO:0000269|PubMed:17613531, ECO:0000269|PubMed:18986166, ECO:0000269|PubMed:19321446, ECO:0007744|PDB:2G54, ECO:0007744|PDB:2JG4, ECO:0007744|PDB:3CWW, ECO:0007744|PDB:3N56, ECO:0007744|PDB:3N57
source Swiss-Prot : SWS_FT_FI2

69) chain A
residue 108
type BINDING
sequence H
description BINDING => ECO:0000255|PROSITE-ProRule:PRU10096, ECO:0000269|PubMed:17051221, ECO:0000269|PubMed:17613531, ECO:0000269|PubMed:18986166, ECO:0000269|PubMed:19321446, ECO:0007744|PDB:2G54, ECO:0007744|PDB:2JG4, ECO:0007744|PDB:3CWW, ECO:0007744|PDB:3N56, ECO:0007744|PDB:3N57
source Swiss-Prot : SWS_FT_FI2

70) chain A
residue 112
type BINDING
sequence H
description BINDING => ECO:0000255|PROSITE-ProRule:PRU10096, ECO:0000269|PubMed:17051221, ECO:0000269|PubMed:17613531, ECO:0000269|PubMed:18986166, ECO:0000269|PubMed:19321446, ECO:0007744|PDB:2G54, ECO:0007744|PDB:2JG4, ECO:0007744|PDB:3CWW, ECO:0007744|PDB:3N56, ECO:0007744|PDB:3N57
source Swiss-Prot : SWS_FT_FI2

71) chain A
residue 189
type BINDING
sequence E
description BINDING => ECO:0000255|PROSITE-ProRule:PRU10096, ECO:0000269|PubMed:17051221, ECO:0000269|PubMed:17613531, ECO:0000269|PubMed:18986166, ECO:0000269|PubMed:19321446, ECO:0007744|PDB:2G54, ECO:0007744|PDB:2JG4, ECO:0007744|PDB:3CWW, ECO:0007744|PDB:3N56, ECO:0007744|PDB:3N57
source Swiss-Prot : SWS_FT_FI2

72) chain B
residue 108
type BINDING
sequence H
description BINDING => ECO:0000255|PROSITE-ProRule:PRU10096, ECO:0000269|PubMed:17051221, ECO:0000269|PubMed:17613531, ECO:0000269|PubMed:18986166, ECO:0000269|PubMed:19321446, ECO:0007744|PDB:2G54, ECO:0007744|PDB:2JG4, ECO:0007744|PDB:3CWW, ECO:0007744|PDB:3N56, ECO:0007744|PDB:3N57
source Swiss-Prot : SWS_FT_FI2

73) chain B
residue 112
type BINDING
sequence H
description BINDING => ECO:0000255|PROSITE-ProRule:PRU10096, ECO:0000269|PubMed:17051221, ECO:0000269|PubMed:17613531, ECO:0000269|PubMed:18986166, ECO:0000269|PubMed:19321446, ECO:0007744|PDB:2G54, ECO:0007744|PDB:2JG4, ECO:0007744|PDB:3CWW, ECO:0007744|PDB:3N56, ECO:0007744|PDB:3N57
source Swiss-Prot : SWS_FT_FI2

74) chain B
residue 189
type BINDING
sequence E
description BINDING => ECO:0000255|PROSITE-ProRule:PRU10096, ECO:0000269|PubMed:17051221, ECO:0000269|PubMed:17613531, ECO:0000269|PubMed:18986166, ECO:0000269|PubMed:19321446, ECO:0007744|PDB:2G54, ECO:0007744|PDB:2JG4, ECO:0007744|PDB:3CWW, ECO:0007744|PDB:3N56, ECO:0007744|PDB:3N57
source Swiss-Prot : SWS_FT_FI2

75) chain C
residue 108
type BINDING
sequence H
description BINDING => ECO:0000255|PROSITE-ProRule:PRU10096, ECO:0000269|PubMed:17051221, ECO:0000269|PubMed:17613531, ECO:0000269|PubMed:18986166, ECO:0000269|PubMed:19321446, ECO:0007744|PDB:2G54, ECO:0007744|PDB:2JG4, ECO:0007744|PDB:3CWW, ECO:0007744|PDB:3N56, ECO:0007744|PDB:3N57
source Swiss-Prot : SWS_FT_FI2

76) chain C
residue 112
type BINDING
sequence H
description BINDING => ECO:0000255|PROSITE-ProRule:PRU10096, ECO:0000269|PubMed:17051221, ECO:0000269|PubMed:17613531, ECO:0000269|PubMed:18986166, ECO:0000269|PubMed:19321446, ECO:0007744|PDB:2G54, ECO:0007744|PDB:2JG4, ECO:0007744|PDB:3CWW, ECO:0007744|PDB:3N56, ECO:0007744|PDB:3N57
source Swiss-Prot : SWS_FT_FI2

77) chain A
residue 336
type BINDING
sequence H
description in the exosite
source Swiss-Prot : SWS_FT_FI3

78) chain B
residue 336
type BINDING
sequence H
description in the exosite
source Swiss-Prot : SWS_FT_FI3

79) chain C
residue 336
type BINDING
sequence H
description in the exosite
source Swiss-Prot : SWS_FT_FI3

80) chain D
residue 336
type BINDING
sequence H
description in the exosite
source Swiss-Prot : SWS_FT_FI3

81) chain E
residue 336
type BINDING
sequence H
description in the exosite
source Swiss-Prot : SWS_FT_FI3

82) chain F
residue 336
type BINDING
sequence H
description in the exosite
source Swiss-Prot : SWS_FT_FI3

83) chain G
residue 336
type BINDING
sequence H
description in the exosite
source Swiss-Prot : SWS_FT_FI3

84) chain H
residue 336
type BINDING
sequence H
description in the exosite
source Swiss-Prot : SWS_FT_FI3

85) chain A
residue 359
type BINDING
sequence L
description BINDING => ECO:0000269|PubMed:18986166
source Swiss-Prot : SWS_FT_FI4

86) chain B
residue 359
type BINDING
sequence L
description BINDING => ECO:0000269|PubMed:18986166
source Swiss-Prot : SWS_FT_FI4

87) chain C
residue 359
type BINDING
sequence L
description BINDING => ECO:0000269|PubMed:18986166
source Swiss-Prot : SWS_FT_FI4

88) chain D
residue 359
type BINDING
sequence L
description BINDING => ECO:0000269|PubMed:18986166
source Swiss-Prot : SWS_FT_FI4

89) chain E
residue 359
type BINDING
sequence L
description BINDING => ECO:0000269|PubMed:18986166
source Swiss-Prot : SWS_FT_FI4

90) chain F
residue 359
type BINDING
sequence L
description BINDING => ECO:0000269|PubMed:18986166
source Swiss-Prot : SWS_FT_FI4

91) chain G
residue 359
type BINDING
sequence L
description BINDING => ECO:0000269|PubMed:18986166
source Swiss-Prot : SWS_FT_FI4

92) chain H
residue 359
type BINDING
sequence L
description BINDING => ECO:0000269|PubMed:18986166
source Swiss-Prot : SWS_FT_FI4

93) chain A
residue 429
type BINDING
sequence R
description BINDING => ECO:0000250|UniProtKB:P35559
source Swiss-Prot : SWS_FT_FI5

94) chain A
residue 895
type BINDING
sequence D
description BINDING => ECO:0000250|UniProtKB:P35559
source Swiss-Prot : SWS_FT_FI5

95) chain B
residue 429
type BINDING
sequence R
description BINDING => ECO:0000250|UniProtKB:P35559
source Swiss-Prot : SWS_FT_FI5

96) chain B
residue 895
type BINDING
sequence D
description BINDING => ECO:0000250|UniProtKB:P35559
source Swiss-Prot : SWS_FT_FI5

97) chain C
residue 429
type BINDING
sequence R
description BINDING => ECO:0000250|UniProtKB:P35559
source Swiss-Prot : SWS_FT_FI5

98) chain C
residue 895
type BINDING
sequence D
description BINDING => ECO:0000250|UniProtKB:P35559
source Swiss-Prot : SWS_FT_FI5

99) chain D
residue 429
type BINDING
sequence R
description BINDING => ECO:0000250|UniProtKB:P35559
source Swiss-Prot : SWS_FT_FI5

100) chain D
residue 895
type BINDING
sequence D
description BINDING => ECO:0000250|UniProtKB:P35559
source Swiss-Prot : SWS_FT_FI5

101) chain E
residue 429
type BINDING
sequence R
description BINDING => ECO:0000250|UniProtKB:P35559
source Swiss-Prot : SWS_FT_FI5

102) chain E
residue 895
type BINDING
sequence D
description BINDING => ECO:0000250|UniProtKB:P35559
source Swiss-Prot : SWS_FT_FI5

103) chain F
residue 429
type BINDING
sequence R
description BINDING => ECO:0000250|UniProtKB:P35559
source Swiss-Prot : SWS_FT_FI5

104) chain F
residue 895
type BINDING
sequence D
description BINDING => ECO:0000250|UniProtKB:P35559
source Swiss-Prot : SWS_FT_FI5

105) chain G
residue 429
type BINDING
sequence R
description BINDING => ECO:0000250|UniProtKB:P35559
source Swiss-Prot : SWS_FT_FI5

106) chain G
residue 895
type BINDING
sequence D
description BINDING => ECO:0000250|UniProtKB:P35559
source Swiss-Prot : SWS_FT_FI5

107) chain H
residue 429
type BINDING
sequence R
description BINDING => ECO:0000250|UniProtKB:P35559
source Swiss-Prot : SWS_FT_FI5

108) chain H
residue 895
type BINDING
sequence D
description BINDING => ECO:0000250|UniProtKB:P35559
source Swiss-Prot : SWS_FT_FI5


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