eF-site ID 4j3j-A
PDB Code 4j3j
Chain A

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Title Crystal Structure of DPP-IV with Compound C3
Classification HYDROLASE/HYDROLASE INHIBITOR
Compound Dipeptidyl peptidase 4
Source Homo sapiens (Human) (DPP4_HUMAN)
Sequence A:  RKTYTLTDYLKNTYRLKLYSLRWISDHEYLYKQENNILVF
NAEYGNSSVFLENSTFDEFGHSINDYSISPDGQFILLEYN
YVKQWRHSYTASYDIYDLNKRQLITEERIPNNTQWVTWSP
VGHKLAYVWNNDIYVKIEPNLPSYRITWTGKEDIIYNGIT
DWVYEEEVFSAYSALWWSPNGTFLAYAQFNDTEVPLIEYS
FYSDESLQYPKTVRVPYPKAGAVNPTVKFFVVNTDSLSSV
TNATSIQITAPASMLIGDHYLCDVTWATQERISLQWLRRI
QNYSVMDICDYDESSGRWNCLVARQHIEMSTTGWVGRFRP
SEPHFTLDGNSFYKIISNEEGYRHICYFQIDKKDCTFITK
GTWEVIGIEALTSDYLYYISNEYKGMPGGRNLYKIQLSDY
TKVTCLSCELNPERCQYYSVSFSKEAKYYQLRCSGPGLPL
YTLHSSVNDKGLRVLEDNSALDKMLQNVQMPSKKLDFIIL
NETKFWYQMILPPHFDKSKKYPLLLDVYAGPCSQKADTVF
RLNWATYLASTENIIVASFDGRGSGYQGDKIMHAINRRLG
TFEVEDQIEAARQFSKMGFVDNKRIAIWGWSYGGYVTSMV
LGSGSGVFKCGIAVAPVSRWEYYDSVYTERYMGLPTPEDN
LDHYRNSTVMSRAENFKQVEYLLIHGTADDNVHFQQSAQI
SKALVDVGVDFQAMWYTDEDHGIASSTAHQHIYTHMSHFI
KQCFS
Description


Functional site

1) chain A
residue 125
type
sequence R
description BINDING SITE FOR RESIDUE D3C A 801
source : AC1

2) chain A
residue 205
type
sequence E
description BINDING SITE FOR RESIDUE D3C A 801
source : AC1

3) chain A
residue 206
type
sequence E
description BINDING SITE FOR RESIDUE D3C A 801
source : AC1

4) chain A
residue 357
type
sequence F
description BINDING SITE FOR RESIDUE D3C A 801
source : AC1

5) chain A
residue 585
type
sequence Y
description BINDING SITE FOR RESIDUE D3C A 801
source : AC1

6) chain A
residue 630
type
sequence S
description BINDING SITE FOR RESIDUE D3C A 801
source : AC1

7) chain A
residue 631
type
sequence Y
description BINDING SITE FOR RESIDUE D3C A 801
source : AC1

8) chain A
residue 656
type
sequence V
description BINDING SITE FOR RESIDUE D3C A 801
source : AC1

9) chain A
residue 662
type
sequence Y
description BINDING SITE FOR RESIDUE D3C A 801
source : AC1

10) chain A
residue 666
type
sequence Y
description BINDING SITE FOR RESIDUE D3C A 801
source : AC1

11) chain A
residue 710
type
sequence N
description BINDING SITE FOR RESIDUE D3C A 801
source : AC1

12) chain A
residue 711
type
sequence V
description BINDING SITE FOR RESIDUE D3C A 801
source : AC1

13) chain A
residue 547
type catalytic
sequence Y
description 169
source MCSA : MCSA1

14) chain A
residue 630
type catalytic
sequence S
description 169
source MCSA : MCSA1

15) chain A
residue 631
type catalytic
sequence Y
description 169
source MCSA : MCSA1

16) chain A
residue 708
type catalytic
sequence D
description 169
source MCSA : MCSA1

17) chain A
residue 740
type catalytic
sequence H
description 169
source MCSA : MCSA1

18) 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

19) 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

20) 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

21) 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

22) 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

23) 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

24) 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

25) chain A
residue 605-635
type prosite
sequence DQIEAARQFSKMGFVDNKRIAIWGWSYGGYV
description PRO_ENDOPEP_SER Prolyl endopeptidase family serine active site. DqieAarqFskmgfvdnkriaiwGwSyGGYV
source prosite : PS00708

26) chain A
residue 630
type ACT_SITE
sequence S
description Charge relay system => ECO:0000255|PROSITE-ProRule:PRU10084
source Swiss-Prot : SWS_FT_FI1

27) chain A
residue 708
type ACT_SITE
sequence D
description Charge relay system => ECO:0000255|PROSITE-ProRule:PRU10084
source Swiss-Prot : SWS_FT_FI1

28) chain A
residue 740
type ACT_SITE
sequence H
description Charge relay system => ECO:0000255|PROSITE-ProRule:PRU10084
source Swiss-Prot : SWS_FT_FI1

29) 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

30) 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


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