eF-site ID 2g54-ABCD
PDB Code 2g54
Chain A, B, C, D

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Title Crystal structure of Zn-bound human insulin-degrading enzyme in complex with insulin B chain
Classification HYDROLASE
Compound Insulin-degrading enzyme
Source null (INS_HUMAN)
Sequence A:  NNPAIKRIGNHITKSPEDKREYRGLELANGIKVLLISDPT
TDKSSAALDVHIGSLSDPPNIAGLSHFCQHMLFLGTKKYP
KENEYSQFLSEHAGSSNAFTSGEHTNYYFDVSHEHLEGAL
DRFAQFFLCPLFDESCKDREVNAVDSEHEKNVMNDAWRLF
QLEKATGNPKHPFSKFGTGNKYTLETRPNQEGIDVRQELL
KFHSAYYSSNLMAVCVLGRESLDDLTNLVVKLFSEVENKN
VPLPEFPEHPFQEEHLKQLYKIVPIKDIRNLYVTFPIPDL
QKYYKSNPGHYLGHLIGHEGPGSLLSELKSKGWVNTLVGG
QKEGARGFMFFIINVDLTEEGLLHVEDIILHMFQYIQKLR
AEGPQEWVFQECKDLNAVAFRFKDKERPRGYTSKIAGILH
YYPLEEVLTAEYLLEEFRPDLIEMVLDKLRPENVRVAIVS
KSFEGKTDRTEEWYGTQYKQEAIPDEVIKKWQNADLNGKF
KLPTKNEFIPTNFEILPLEKEATPYPALIKDTAMSKLWFK
QDDKFFLPKACLNFEFFSPFAYVDPLHCNMAYLYLELLKD
SLNEYAYAAELAGLSYDLQNTIYGMYLSVKGYNDKQPILL
KKIIEKMATFEIDEKRFEIIKEAYMRSLNNFRAEQPHQHA
MYYLRLLMTEVAWTKDELKEALDDVTLPRLKAFIPQLLSR
LHIEALLHGNITKQAALGIMQMVEDTLIEHAHTKPLLPSQ
LVRYREVQLPDRGWFVYQQRNEVHNNCGIEIYYQTDMQST
SENMFLELFCQIISEPCFNTLRTKEQLGYIVFSGPRRANG
IQGLRFIIQSEKPPHYLESRVEAFLITMEKSIEDMTEEAF
QKHIQALAIRRLDKPKKLSAECAKYWGEIISQQYNFDRDN
TEVAYLKTLTKEDIIKFYKEMLAVDAPRRHKVSVHVLARE
MDSCPVVGENDINLSQAPALPQPEVIQNMTEFKRGLPLFP
LVKPHINFMA
B:  NPAIKRIGNHITKSPEDKREYRGLELANGIKVLLISDPTT
DKSSAALDVHIGSLSDPPNIAGLSHFCQHMLFLGTKKYPK
ENEYSQFLSEHAGSSNAFTSGEHTNYYFDVSHEHLEGALD
RFAQFFLCPLFDESCKDREVNAVDSEHEKNVMNDAWRLFQ
LEKATGNPKHPFSKFGTGNKYTLETRPNQEGIDVRQELLK
FHSAYYSSNLMAVCVLGRESLDDLTNLVVKLFSEVENKNV
PLPEFPEHPFQEEHLKQLYKIVPIKDIRNLYVTFPIPDLQ
KYYKSNPGHYLGHLIGHEGPGSLLSELKSKGWVNTLVGGQ
KEGARGFMFFIINVDLTEEGLLHVEDIILHMFQYIQKLRA
EGPQEWVFQECKDLNAVAFRFKDKERPRGYTSKIAGILHY
YPLEEVLTAEYLLEEFRPDLIEMVLDKLRPENVRVAIVSK
SFEGKTDRTEEWYGTQYKQEAIPDEVIKKWQNADLNGKFK
LPTKNEFIPTNFEILPLEKEATPYPALIKDTAMSKLWFKQ
DDKFFLPKACLNFEFFSPFAYVDPLHCNMAYLYLELLKDS
LNEYAYAAELAGLSYDLQNTIYGMYLSVKGYNDKQPILLK
KIIEKMATFEIDEKRFEIIKEAYMRSLNNFRAEQPHQHAM
YYLRLLMTEVAWTKDELKEALDDVTLPRLKAFIPQLLSRL
HIEALLHGNITKQAALGIMQMVEDTLIEHAHTKPLLPSQL
VRYREVQLPDRGWFVYQQRNEVHNNCGIEIYYQTDMQSTS
ENMFLELFCQIISEPCFNTLRTKEQLGYIVFSGPRRANGI
QGLRFIIQSEKPPHYLESRVEAFLITMEKSIEDMTEEAFQ
KHIQALAIRRLDKPKKLSAECAKYWGEIISQQYNFDRDNT
EVAYLKTLTKEDIIKFYKEMLAVDAPRRHKVSVHVLAREM
DSCPVVGEFINLSQAPALPQPEVIQNMTEFKRGLPLFPLV
KPHINF
C:  FVNQHEALYLVCG
D:  FVNQHEALYLVC
Description


Functional site
1) chain A
residue 108
type
sequence H
description BINDING SITE FOR RESIDUE ZN A 1100
source : AC1
2) chain A
residue 112
type
sequence H
description BINDING SITE FOR RESIDUE ZN A 1100
source : AC1
3) chain A
residue 189
type
sequence E
description BINDING SITE FOR RESIDUE ZN A 1100
source : AC1
4) chain C
residue 16
type
sequence Y
description BINDING SITE FOR RESIDUE ZN A 1100
source : AC1
5) chain B
residue 108
type
sequence H
description BINDING SITE FOR RESIDUE ZN B 1200
source : AC2
6) chain B
residue 112
type
sequence H
description BINDING SITE FOR RESIDUE ZN B 1200
source : AC2
7) chain B
residue 189
type
sequence E
description BINDING SITE FOR RESIDUE ZN B 1200
source : AC2
8) chain D
residue 16
type
sequence Y
description BINDING SITE FOR RESIDUE ZN B 1200
source : AC2
9) chain A
residue 204
type
sequence L
description BINDING SITE FOR RESIDUE DIO A 2000
source : AC3
10) chain A
residue 205
type
sequence E
description BINDING SITE FOR RESIDUE DIO A 2000
source : AC3
11) chain A
residue 477
type
sequence R
description BINDING SITE FOR RESIDUE DIO A 2000
source : AC3
12) chain A
residue 479
type
sequence A
description BINDING SITE FOR RESIDUE DIO A 2000
source : AC3
13) chain B
residue 205
type
sequence E
description BINDING SITE FOR RESIDUE DIO B 2001
source : AC4
14) chain B
residue 477
type
sequence R
description BINDING SITE FOR RESIDUE DIO B 2001
source : AC4
15) chain B
residue 479
type
sequence A
description BINDING SITE FOR RESIDUE DIO B 2001
source : AC4
16) 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
17) 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
18) 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
19) 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
20) 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
21) 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
22) 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
23) 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
24) chain A
residue 336
type BINDING
sequence H
description in the exosite
source Swiss-Prot : SWS_FT_FI3
25) chain B
residue 336
type BINDING
sequence H
description in the exosite
source Swiss-Prot : SWS_FT_FI3
26) chain A
residue 359
type BINDING
sequence L
description BINDING => ECO:0000269|PubMed:18986166
source Swiss-Prot : SWS_FT_FI4
27) chain B
residue 359
type BINDING
sequence L
description BINDING => ECO:0000269|PubMed:18986166
source Swiss-Prot : SWS_FT_FI4
28) chain A
residue 429
type BINDING
sequence R
description BINDING => ECO:0000250|UniProtKB:P35559
source Swiss-Prot : SWS_FT_FI5
29) chain A
residue 895
type BINDING
sequence D
description BINDING => ECO:0000250|UniProtKB:P35559
source Swiss-Prot : SWS_FT_FI5
30) chain B
residue 429
type BINDING
sequence R
description BINDING => ECO:0000250|UniProtKB:P35559
source Swiss-Prot : SWS_FT_FI5
31) chain B
residue 895
type BINDING
sequence D
description BINDING => ECO:0000250|UniProtKB:P35559
source Swiss-Prot : SWS_FT_FI5
32) chain A
residue 192
type MOD_RES
sequence K
description N6-succinyllysine => ECO:0000250|UniProtKB:Q9JHR7
source Swiss-Prot : SWS_FT_FI6
33) chain A
residue 697
type MOD_RES
sequence K
description N6-succinyllysine => ECO:0000250|UniProtKB:Q9JHR7
source Swiss-Prot : SWS_FT_FI6
34) chain B
residue 192
type MOD_RES
sequence K
description N6-succinyllysine => ECO:0000250|UniProtKB:Q9JHR7
source Swiss-Prot : SWS_FT_FI6
35) chain B
residue 697
type MOD_RES
sequence K
description N6-succinyllysine => ECO:0000250|UniProtKB:Q9JHR7
source Swiss-Prot : SWS_FT_FI6

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