|
eF-site ID
|
5wob-E |
PDB Code
|
5wob |
Chain
|
E |
|
click to enlarge
|
|
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
|
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
|
|
Description
|
|
Functional site
|
|
1)
|
chain |
E |
residue |
108 |
type |
|
sequence |
H
|
description |
binding site for residue ZN E 2001
|
source |
: AC5
|
|
2)
|
chain |
E |
residue |
112 |
type |
|
sequence |
H
|
description |
binding site for residue ZN E 2001
|
source |
: AC5
|
|
3)
|
chain |
E |
residue |
189 |
type |
|
sequence |
E
|
description |
binding site for residue ZN E 2001
|
source |
: AC5
|
|
4)
|
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
|
|
5)
|
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
|
|
6)
|
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
|
|
7)
|
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
|
|
8)
|
chain |
E |
residue |
336 |
type |
BINDING |
sequence |
H
|
description |
in the exosite
|
source |
Swiss-Prot : SWS_FT_FI3
|
|
9)
|
chain |
E |
residue |
359 |
type |
BINDING |
sequence |
L
|
description |
BINDING => ECO:0000269|PubMed:18986166
|
source |
Swiss-Prot : SWS_FT_FI4
|
|
10)
|
chain |
E |
residue |
895 |
type |
BINDING |
sequence |
D
|
description |
BINDING => ECO:0000250|UniProtKB:P35559
|
source |
Swiss-Prot : SWS_FT_FI5
|
|
11)
|
chain |
E |
residue |
429 |
type |
BINDING |
sequence |
R
|
description |
BINDING => ECO:0000250|UniProtKB:P35559
|
source |
Swiss-Prot : SWS_FT_FI5
|
|
12)
|
chain |
E |
residue |
697 |
type |
MOD_RES |
sequence |
K
|
description |
N6-succinyllysine => ECO:0000250|UniProtKB:Q9JHR7
|
source |
Swiss-Prot : SWS_FT_FI6
|
|
13)
|
chain |
E |
residue |
192 |
type |
MOD_RES |
sequence |
K
|
description |
N6-succinyllysine => ECO:0000250|UniProtKB:Q9JHR7
|
source |
Swiss-Prot : SWS_FT_FI6
|
|
|
|