eF-site ID 2oqv-AB
PDB Code 2oqv
Chain A, B

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Title Human Dipeptidyl Peptidase IV (DPP4) with piperidine-constrained phenethylamine
Classification HYDROLASE
Compound Dipeptidyl peptidase 4 (Dipeptidyl peptidase IV) (DPP IV)
Source Homo sapiens (Human) (DPP4_HUMAN)
Sequence A:  SRKTYTLTDYLKNTYRLKLYSLRWISDHEYLYKQENNILV
FNAEYGNSSVFLENSTFDEFGHSINDYSISPDGQFILLEY
NYVKQWRHSYTASYDIYDLNKRQLITEERIPNNTQWVTWS
PVGHKLAYVWNNDIYVKIEPNLPSYRITWTGKEDIIYNGI
TDWVYEEEVFSAYSALWWSPNGTFLAYAQFNDTEVPLIEY
SFYSDESLQYPKTVRVPYPKAGAVNPTVKFFVVNTDSLSS
VTNATSIQITAPASMLIGDHYLCDVTWATQERISLQWLRR
IQNYSVMDICDYDESSGRWNCLVARQHIEMSTTGWVGRFR
PSEPHFTLDGNSFYKIISNEEGYRHICYFQIDKKDCTFIT
KGTWEVIGIEALTSDYLYYISNEYKGMPGGRNLYKIQLSD
YTKVTCLSCELNPERCQYYSVSFSKEAKYYQLRCSGPGLP
LYTLHSSVNDKGLRVLEDNSALDKMLQNVQMPSKKLDFII
LNETKFWYQMILPPHFDKSKKYPLLLDVYAGPCSQKADTV
FRLNWATYLASTENIIVASFDGRGSGYQGDKIMHAINRRL
GTFEVEDQIEAARQFSKMGFVDNKRIAIWGWSYGGYVTSM
VLGSGSGVFKCGIAVAPVSRWEYYDSVYTERYMGLPTPED
NLDHYRNSTVMSRAENFKQVEYLLIHGTADDNVHFQQSAQ
ISKALVDVGVDFQAMWYTDEDHGIASSTAHQHIYTHMSHF
IKQCFS
B:  SRKTYTLTDYLKNTYRLKLYSLRWISDHEYLYKQENNILV
FNAEYGNSSVFLENSTFDEFGHSINDYSISPDGQFILLEY
NYVKQWRHSYTASYDIYDLNKRQLITEERIPNNTQWVTWS
PVGHKLAYVWNNDIYVKIEPNLPSYRITWTGKEDIIYNGI
TDWVYEEEVFSAYSALWWSPNGTFLAYAQFNDTEVPLIEY
SFYSDESLQYPKTVRVPYPKAGAVNPTVKFFVVNTDSLSS
VTNATSIQITAPASMLIGDHYLCDVTWATQERISLQWLRR
IQNYSVMDICDYDESSGRWNCLVARQHIEMSTTGWVGRFR
PSEPHFTLDGNSFYKIISNEEGYRHICYFQIDKKDCTFIT
KGTWEVIGIEALTSDYLYYISNEYKGMPGGRNLYKIQLSD
YTKVTCLSCELNPERCQYYSVSFSKEAKYYQLRCSGPGLP
LYTLHSSVNDKGLRVLEDNSALDKMLQNVQMPSKKLDFII
LNETKFWYQMILPPHFDKSKKYPLLLDVYAGPCSQKADTV
FRLNWATYLASTENIIVASFDGRGSGYQGDKIMHAINRRL
GTFEVEDQIEAARQFSKMGFVDNKRIAIWGWSYGGYVTSM
VLGSGSGVFKCGIAVAPVSRWEYYDSVYTERYMGLPTPED
NLDHYRNSTVMSRAENFKQVEYLLIHGTADDNVHFQQSAQ
ISKALVDVGVDFQAMWYTDEDHGIASSTAHQHIYTHMSHF
IKQCFS
Description


Functional site
1) chain A
residue 125
type
sequence R
description BINDING SITE FOR RESIDUE MA9 A 901
source : AC1
2) chain A
residue 205
type
sequence E
description BINDING SITE FOR RESIDUE MA9 A 901
source : AC1
3) chain A
residue 206
type
sequence E
description BINDING SITE FOR RESIDUE MA9 A 901
source : AC1
4) chain A
residue 207
type
sequence V
description BINDING SITE FOR RESIDUE MA9 A 901
source : AC1
5) chain A
residue 209
type
sequence S
description BINDING SITE FOR RESIDUE MA9 A 901
source : AC1
6) chain A
residue 357
type
sequence F
description BINDING SITE FOR RESIDUE MA9 A 901
source : AC1
7) chain A
residue 358
type
sequence R
description BINDING SITE FOR RESIDUE MA9 A 901
source : AC1
8) chain A
residue 547
type
sequence Y
description BINDING SITE FOR RESIDUE MA9 A 901
source : AC1
9) chain A
residue 631
type
sequence Y
description BINDING SITE FOR RESIDUE MA9 A 901
source : AC1
10) chain A
residue 656
type
sequence V
description BINDING SITE FOR RESIDUE MA9 A 901
source : AC1
11) chain A
residue 662
type
sequence Y
description BINDING SITE FOR RESIDUE MA9 A 901
source : AC1
12) chain A
residue 666
type
sequence Y
description BINDING SITE FOR RESIDUE MA9 A 901
source : AC1
13) chain A
residue 710
type
sequence N
description BINDING SITE FOR RESIDUE MA9 A 901
source : AC1
14) chain A
residue 711
type
sequence V
description BINDING SITE FOR RESIDUE MA9 A 901
source : AC1
15) chain A
residue 547
type catalytic
sequence Y
description 169
source MCSA : MCSA1
16) chain A
residue 630
type catalytic
sequence S
description 169
source MCSA : MCSA1
17) chain A
residue 631
type catalytic
sequence Y
description 169
source MCSA : MCSA1
18) chain A
residue 708
type catalytic
sequence D
description 169
source MCSA : MCSA1
19) chain A
residue 740
type catalytic
sequence H
description 169
source MCSA : MCSA1
20) chain B
residue 547
type catalytic
sequence Y
description 169
source MCSA : MCSA2
21) chain B
residue 630
type catalytic
sequence S
description 169
source MCSA : MCSA2
22) chain B
residue 631
type catalytic
sequence Y
description 169
source MCSA : MCSA2
23) chain B
residue 708
type catalytic
sequence D
description 169
source MCSA : MCSA2
24) chain B
residue 740
type catalytic
sequence H
description 169
source MCSA : MCSA2
25) chain A
residue 630
type ACT_SITE
sequence S
description Charge relay system => ECO:0000255|PROSITE-ProRule:PRU10084
source Swiss-Prot : SWS_FT_FI1
26) chain A
residue 708
type ACT_SITE
sequence D
description Charge relay system => ECO:0000255|PROSITE-ProRule:PRU10084
source Swiss-Prot : SWS_FT_FI1
27) chain A
residue 740
type ACT_SITE
sequence H
description Charge relay system => ECO:0000255|PROSITE-ProRule:PRU10084
source Swiss-Prot : SWS_FT_FI1
28) chain B
residue 630
type ACT_SITE
sequence S
description Charge relay system => ECO:0000255|PROSITE-ProRule:PRU10084
source Swiss-Prot : SWS_FT_FI1
29) chain B
residue 708
type ACT_SITE
sequence D
description Charge relay system => ECO:0000255|PROSITE-ProRule:PRU10084
source Swiss-Prot : SWS_FT_FI1
30) chain B
residue 740
type ACT_SITE
sequence H
description Charge relay system => ECO:0000255|PROSITE-ProRule:PRU10084
source Swiss-Prot : SWS_FT_FI1
31) chain A
residue 85
type CARBOHYD
sequence N
description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:12483204, ECO:0000269|PubMed:12646248, ECO:0000269|PubMed:12906826, ECO:0000269|PubMed:20684603, ECO:0000269|PubMed:23835475, ECO:0007744|PDB:4L72
source Swiss-Prot : SWS_FT_FI2
32) chain A
residue 229
type CARBOHYD
sequence N
description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:12483204, ECO:0000269|PubMed:12646248, ECO:0000269|PubMed:12906826, ECO:0000269|PubMed:20684603, ECO:0000269|PubMed:23835475, ECO:0007744|PDB:4L72
source Swiss-Prot : SWS_FT_FI2
33) chain B
residue 85
type CARBOHYD
sequence N
description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:12483204, ECO:0000269|PubMed:12646248, ECO:0000269|PubMed:12906826, ECO:0000269|PubMed:20684603, ECO:0000269|PubMed:23835475, ECO:0007744|PDB:4L72
source Swiss-Prot : SWS_FT_FI2
34) chain B
residue 229
type CARBOHYD
sequence N
description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:12483204, ECO:0000269|PubMed:12646248, ECO:0000269|PubMed:12906826, ECO:0000269|PubMed:20684603, ECO:0000269|PubMed:23835475, ECO:0007744|PDB:4L72
source Swiss-Prot : SWS_FT_FI2
35) chain A
residue 92
type CARBOHYD
sequence N
description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:20684603, ECO:0000269|PubMed:23835475, ECO:0007744|PDB:4L72
source Swiss-Prot : SWS_FT_FI3
36) chain B
residue 92
type CARBOHYD
sequence N
description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:20684603, ECO:0000269|PubMed:23835475, ECO:0007744|PDB:4L72
source Swiss-Prot : SWS_FT_FI3
37) chain A
residue 150
type CARBOHYD
sequence N
description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:12483204, ECO:0000269|PubMed:12906826, ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:20684603, ECO:0000269|PubMed:23835475, ECO:0007744|PDB:4L72
source Swiss-Prot : SWS_FT_FI4
38) chain B
residue 150
type CARBOHYD
sequence N
description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:12483204, ECO:0000269|PubMed:12906826, ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:20684603, ECO:0000269|PubMed:23835475, ECO:0007744|PDB:4L72
source Swiss-Prot : SWS_FT_FI4
39) chain A
residue 219
type CARBOHYD
sequence N
description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:12483204, ECO:0000269|PubMed:12646248, ECO:0000269|PubMed:20684603, ECO:0000269|PubMed:23835475, ECO:0007744|PDB:4L72
source Swiss-Prot : SWS_FT_FI5
40) chain B
residue 219
type CARBOHYD
sequence N
description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:12483204, ECO:0000269|PubMed:12646248, ECO:0000269|PubMed:20684603, ECO:0000269|PubMed:23835475, ECO:0007744|PDB:4L72
source Swiss-Prot : SWS_FT_FI5
41) chain A
residue 281
type CARBOHYD
sequence N
description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:12483204, ECO:0000269|PubMed:12646248, ECO:0000269|PubMed:12906826, ECO:0000269|PubMed:23835475, ECO:0007744|PDB:4L72
source Swiss-Prot : SWS_FT_FI6
42) chain B
residue 281
type CARBOHYD
sequence N
description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:12483204, ECO:0000269|PubMed:12646248, ECO:0000269|PubMed:12906826, ECO:0000269|PubMed:23835475, ECO:0007744|PDB:4L72
source Swiss-Prot : SWS_FT_FI6
43) chain A
residue 321
type CARBOHYD
sequence N
description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:12483204, ECO:0000269|PubMed:12646248, ECO:0000269|PubMed:23835475, ECO:0007744|PDB:4L72
source Swiss-Prot : SWS_FT_FI7
44) chain B
residue 321
type CARBOHYD
sequence N
description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:12483204, ECO:0000269|PubMed:12646248, ECO:0000269|PubMed:23835475, ECO:0007744|PDB:4L72
source Swiss-Prot : SWS_FT_FI7
45) chain A
residue 520
type CARBOHYD
sequence N
description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:12483204, ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:20684603, ECO:0000269|PubMed:23835475, ECO:0007744|PDB:4L72
source Swiss-Prot : SWS_FT_FI8
46) chain B
residue 520
type CARBOHYD
sequence N
description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:12483204, ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:20684603, ECO:0000269|PubMed:23835475, ECO:0007744|PDB:4L72
source Swiss-Prot : SWS_FT_FI8
47) chain A
residue 685
type CARBOHYD
sequence N
description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:19159218
source Swiss-Prot : SWS_FT_FI9
48) chain B
residue 685
type CARBOHYD
sequence N
description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:19159218
source Swiss-Prot : SWS_FT_FI9
49) chain A
residue 605-635
type prosite
sequence DQIEAARQFSKMGFVDNKRIAIWGWSYGGYV
description PRO_ENDOPEP_SER Prolyl endopeptidase family serine active site. DqieAarqFskmgfvdnkriaiwGwSyGGYV
source prosite : PS00708

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