eF-site ID 2jg4-B
PDB Code 2jg4
Chain B

click to enlarge
Title Substrate-free IDE structure in its closed conformation
Classification HYDROLASE
Compound INSULIN DEGRADING ENZYME
Source (IDE_HUMAN)
Sequence B:  PAIKRIGNHITKSPEDKREYRGLELANGIKVLLISDPTTD
KSSAALDVHIGSLSDPPNIAGLSHFCEHMLFLGTKKYPKE
NEYSQFLSEHAGSSNAFTSGEHTNYYFDVSHEHLEGALDR
FAQFFLCPLFDESCKDREVNAVDSEHEKNVMNDAWRLFQL
EKATGNPKHPFSKFGTGNKYTLETRPNQEGIDVRQELLKF
HSAYYSSNLMAVCVLGRESLDDLTNLVVKLFSEVENKNVP
LPEFPEHPFQEEHLKQLYKIVPIKDIRNLYVTFPIPDLQK
YYKSNPGHYLGHLIGHEGPGSLLSELKSKGWVNTLVGGQK
EGARGFMFFIINVDLTEEGLLHVEDIILHMFQYIQKLRAE
GPQEWVFQECKDLNAVAFRFKDKERPRGYTSKIAGILHYY
PLEEVLTAEYLLEEFRPDLIEMVLDKLRPENVRVAIVSKS
FEGKTDRTEEWYGTQYKQEAIPDEVIKKWQNADLNGKFKL
PTKNEFIPTNFEILPLEKEATPYPALIKDTAMSKLWFKQD
DKFFLPKACLNFEFFSPFAYVDPLHCNMAYLYLELLKDSL
NEYAYAAELAGLSYDLQNTIYGMYLSVKGYNDKQPILLKK
IIEKMATFEIDEKRFEIIKEAYMRSLNNFRAEQPHQHAMY
YLRLLMTEVAWTKDELKEALDDVTLPRLKAFIPQLLSRLH
IEALLHGNITKQAALGIMQMVEDTLIEHAHTKPLLPSQLV
RYREVQLPDRGWFVYQQRNEVHNNCGIEIYYQTDMQSTSE
NMFLELFCQIISEPCFNTLRTKEQLGFIVFSGPRRANGIQ
GLRFIIQSEKPPHYLESRVEAFLITMEKSIEDMTEEAFQK
HIQALAIRRLDKPKKLSAECAKYWGEIISQQYNFDRDNTE
VAYLKTLTKEDIIKFYKEMLAVDAPRRHKVSVHVLAREMS
CPVVGNLSQAPALPQPEVIQNMTEFKRGLPLFPLVKPH
Description


Functional site

1) chain B
residue 108
type
sequence H
description BINDING SITE FOR RESIDUE ZN B2012
source : AC2

2) chain B
residue 112
type
sequence H
description BINDING SITE FOR RESIDUE ZN B2012
source : AC2

3) chain B
residue 189
type
sequence E
description BINDING SITE FOR RESIDUE ZN B2012
source : AC2

4) chain B
residue 201
type
sequence L
description BINDING SITE FOR RESIDUE DIO B2013
source : AC3

5) chain B
residue 205
type
sequence E
description BINDING SITE FOR RESIDUE DIO B2013
source : AC3

6) chain B
residue 208
type
sequence T
description BINDING SITE FOR RESIDUE DIO B2013
source : AC3

7) chain B
residue 477
type
sequence R
description BINDING SITE FOR RESIDUE DIO B2013
source : AC3

8) chain B
residue 800
type
sequence Q
description BINDING SITE FOR RESIDUE DIO B2014
source : AC6

9) chain B
residue 839
type
sequence R
description BINDING SITE FOR RESIDUE DIO B2014
source : AC6

10) chain B
residue 841
type
sequence N
description BINDING SITE FOR RESIDUE DIO B2014
source : AC6

11) chain B
residue 842
type
sequence G
description BINDING SITE FOR RESIDUE DIO B2014
source : AC6

12) chain B
residue 112
type ACT_SITE
sequence H
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

13) chain B
residue 109
type BINDING
sequence F
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

14) chain B
residue 113
type BINDING
sequence M
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

15) chain B
residue 190
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

16) chain B
residue 337
type BINDING
sequence L
description in the exosite
source Swiss-Prot : SWS_FT_FI3

17) chain B
residue 360
type BINDING
sequence V
description BINDING => ECO:0000269|PubMed:18986166
source Swiss-Prot : SWS_FT_FI4

18) chain B
residue 430
type BINDING
sequence P
description BINDING => ECO:0000250|UniProtKB:P35559
source Swiss-Prot : SWS_FT_FI5

19) chain B
residue 896
type BINDING
sequence K
description BINDING => ECO:0000250|UniProtKB:P35559
source Swiss-Prot : SWS_FT_FI5

20) chain B
residue 193
type MOD_RES
sequence N
description N6-succinyllysine => ECO:0000250|UniProtKB:Q9JHR7
source Swiss-Prot : SWS_FT_FI6

21) chain B
residue 698
type MOD_RES
sequence D
description N6-succinyllysine => ECO:0000250|UniProtKB:Q9JHR7
source Swiss-Prot : SWS_FT_FI6


Display surface

Download
Links