|
eF-site ID
|
5t4h-A |
PDB Code
|
5t4h |
Chain
|
A |
|
click to enlarge
|
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Title
|
Human DPP4 in complex with ligand 34n |
Classification
|
Hydrolase/Hydrolase Inhibitor |
Compound
|
Dipeptidyl peptidase 4 |
Source
|
(DPP4_HUMAN) |
|
Sequence
|
A: |
TRKTYTLTDYLKNTYRLKLYSLRWISDHEYLYKQENNILV
FNAEYGNSSVFLENSTFDEFGHSINDYSISPDGQFILLEY
NYVKQWRHSYTASYDIYDLNKRQLITEERIPNNTQWVTWS
PVGHKLAYVWNNDIYVKIEPNLPSYRITWTGKEDIIYNGI
TDWVYEEEVFSAYSALWWSPNGTFLAYAQFNDTEVPLIEY
SFYSDESLQYPKTVRVPYPKAGAVNPTVKFFVVNTDSLSS
VTNATSIQITAPASMLIGDHYLCDVTWATQERISLQWLRR
IQNYSVMDICDYDESSGRWNCLVARQHIEMSTTGWVGRFR
PSEPHFTLDGNSFYKIISNEEGYRHICYFQIDKKDCTFIT
KGTWEVIGIEALTSDYLYYISNEYKGMPGGRNLYKIQLSD
YTKVTCLSCELNPERCQYYSVSFSKEAKYYQLRCSGPGLP
LYTLHSSVNDKGLRVLEDNSALDKMLQNVQMPSKKLDFII
LNETKFWYQMILPPHFDKSKKYPLLLDVYAGPCSQKADTV
FRLNWATYLASTENIIVASFDGRGSGYQGDKIMHAINRRL
GTFEVEDQIEAARQFSKMGFVDNKRIAIWGWSYGGYVTSM
VLGSGSGVFKCGIAVAPVSRWEYYDSVYTERYMGLPTPED
NLDHYRNSTVMSRAENFKQVEYLLIHGTADDNVHFQQSAQ
ISKALVDVGVDFQAMWYTDEDHGIASSTAHQHIYTHMSHF
IKQCFSLP
|
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Description
|
|
Functional site
|
|
1)
|
chain |
A |
residue |
547 |
type |
catalytic |
sequence |
Y
|
description |
169
|
source |
MCSA : MCSA1
|
|
2)
|
chain |
A |
residue |
630 |
type |
catalytic |
sequence |
S
|
description |
169
|
source |
MCSA : MCSA1
|
|
3)
|
chain |
A |
residue |
631 |
type |
catalytic |
sequence |
Y
|
description |
169
|
source |
MCSA : MCSA1
|
|
4)
|
chain |
A |
residue |
708 |
type |
catalytic |
sequence |
D
|
description |
169
|
source |
MCSA : MCSA1
|
|
5)
|
chain |
A |
residue |
740 |
type |
catalytic |
sequence |
H
|
description |
169
|
source |
MCSA : MCSA1
|
|
6)
|
chain |
A |
residue |
605-635 |
type |
prosite |
sequence |
DQIEAARQFSKMGFVDNKRIAIWGWSYGGYV
|
description |
PRO_ENDOPEP_SER Prolyl endopeptidase family serine active site. DqieAarqFskmgfvdnkriaiwGwSyGGYV
|
source |
prosite : PS00708
|
|
7)
|
chain |
A |
residue |
630 |
type |
ACT_SITE |
sequence |
S
|
description |
Charge relay system => ECO:0000255|PROSITE-ProRule:PRU10084
|
source |
Swiss-Prot : SWS_FT_FI1
|
|
8)
|
chain |
A |
residue |
708 |
type |
ACT_SITE |
sequence |
D
|
description |
Charge relay system => ECO:0000255|PROSITE-ProRule:PRU10084
|
source |
Swiss-Prot : SWS_FT_FI1
|
|
9)
|
chain |
A |
residue |
740 |
type |
ACT_SITE |
sequence |
H
|
description |
Charge relay system => ECO:0000255|PROSITE-ProRule:PRU10084
|
source |
Swiss-Prot : SWS_FT_FI1
|
|
10)
|
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
|
|
11)
|
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
|
|
12)
|
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
|
|
13)
|
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
|
|
14)
|
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
|
|
15)
|
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
|
|
16)
|
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
|
|
17)
|
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
|
|
18)
|
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
|
|
|
|