eF-site ID 3e50-B
PDB Code 3e50
Chain B

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Title Crystal structure of human insulin degrading enzyme in complex with transforming growth factor-alpha
Classification Hydrolase/Hormone
Compound Insulin-degrading enzyme
Source Homo sapiens (Human) (TGFA_HUMAN)
Sequence B:  PAIKRIGNHITKSPEDKREYRGLELANGIKVLLISDPTTD
KSSAALDVHIGSLSDPPNIAGLSHFCQHMLFLGTKKYPKE
NEYSQFLSEHAGSSNAFTSGEHTNYYFDVSHEHLEGALDR
FAQFFLCPLFDESCKDREVNAVDSEHEKNVMNDAWRLFQL
EKATGNPKHPFSKFGTGNKYTLETRPNQEGIDVRQELLKF
HSAYYSSNLMAVCVLGRESLDDLTNLVVKLFSEVENKNVP
LPEFPEHPQEEHLKQLYKIVPIKDIRNLYVTFPIPDLQKY
YKSNPGHYLGHLIGHEGPGSLLSELKSKGWVNTLVGGQKE
GARGFMFFIINVDLTEEGLLHVEDIILHMFQYIQKLRAEG
PQEWVFQECKDLNAVAFRFKDKERPRGYTSKIAGILHYYP
LEEVLTAEYLLEEFRPDLIEMVLDKLRPENVRVAIVSKSF
EGKTDRTEEWYGTQYKQEAIPDEVIKKWQNADLNGKFKLP
TKNEFIPTNFEILPLEKEATPYPALIKDTAMSKLWFKQDD
KFFLPKACLNFEFFSPFAYVDPLHCNMALYLELLKDSLNE
YAYAAELAGLSYDLQNTIYGMYLSVKGYNDKQPILLKKII
EKMATFEIDEKRFEIIKEAYMRSLNNFRAEQPHQHAMYYL
RLLMTEVAWTKDELKEALDDVTLPRLKAFIPQLLSRLHIE
ALLHGNITKQAALGIMQMVEDTLIEHAHTKPLLPSQLVRY
REVQLPDRGWFVYQQRNEVHNNCGIEIYYQTDMQSTSENM
FLELFCQIISEPCFNTLRTKEQLGYIVFSGPRRANGQGLR
FIIQSEKPPHYLESRVEAFLITMEKSIEDMTEEAFQKHIQ
ALAIRRLDKPKKLSAECAKYWGEIISQQYNFDRDNTEVAY
LKTLTKEDIIKFYKEMLAVDAPRRHKVSVHVLAREMSCPV
VGNLSQAPALPQPEVIQNMTEFKRGLPLFPLVKPH
Description


Functional site

1) chain B
residue 108
type
sequence H
description BINDING SITE FOR RESIDUE ZN D 51
source : AC2

2) chain B
residue 112
type
sequence H
description BINDING SITE FOR RESIDUE ZN D 51
source : AC2

3) chain B
residue 189
type
sequence E
description BINDING SITE FOR RESIDUE ZN D 51
source : AC2

4) 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

5) 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

6) 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

7) 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

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

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

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

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

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

13) 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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