eF-site ID 5wob-G
PDB Code 5wob
Chain G

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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 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
Description


Functional site

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

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

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

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

5) 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

6) 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

7) 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

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

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

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

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


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