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eF-site ID
|
2g5p-B |
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PDB Code
|
2g5p |
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Chain
|
B |
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click to enlarge
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Title
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Crystal structure of human dipeptidyl peptidase IV (DPPIV) complexed with cyanopyrrolidine (C5-pro-pro) inhibitor 21ac |
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Classification
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HYDROLASE |
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Compound
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Dipeptidyl peptidase 4 |
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Source
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Homo sapiens (Human) (DPP4_HUMAN) |
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Sequence
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B: |
SRKTYTLTDYLKNTYRLKLYSLRWISDHEYLYKQENNILV
FNAEYGNSSVFLENSTFDEFGHSINDYSISPDGQFILLEY
NYVKQWRHSYTASYDIYDLNKRQLITEERIPNNTQWVTWS
PVGHKLAYVWNNDIYVKIEPNLPSYRITWTGKEDIIYNGI
TDWVYEEEVFSAYSALWWSPNGTFLAYAQFNDTEVPLIEY
SFYSDESLQYPKTVRVPYPKAGAVNPTVKFFVVNTDSLSS
VTNATSIQITAPASMLIGDHYLCDVTWATQERISLQWLRR
IQNYSVMDICDYDESSGRWNCLVARQHIEMSTTGWVGRFR
PSEPHFTLDGNSFYKIISNEEGYRHICYFQIDKKDCTFIT
KGTWEVIGIEALTSDYLYYISNEYKGMPGGRNLYKIQLSD
YTKVTCLSCELNPERCQYYSVSFSKEAKYYQLRCSGPGLP
LYTLHSSVNDKGLRVLEDNSALDKMLQNVQMPSKKLDFII
LNETKFWYQMILPPHFDKSKKYPLLLDVYAGPCSQKADTV
FRLNWATYLASTENIIVASFDGRGSGYQGDKIMHAINRRL
GTFEVEDQIEAARQFSKMGFVDNKRIAIWGWSYGGYVTSM
VLGSGSGVFKCGIAVAPVSRWEYYDSVYTERYMGLPTPED
NLDHYRNSTVMSRAENFKQVEYLLIHGTADDNVHFQQSAQ
ISKALVDVGVDFQAMWYTDEDHGIASSTAHQHIYTHMSHF
IKQCFS
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Description
|
(1) |
Dipeptidyl peptidase 4
|
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Functional site
|
|
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1)
|
chain |
B |
| residue |
547 |
| type |
catalytic |
| sequence |
Y
|
| description |
169
|
| source |
MCSA : MCSA2
|
|
|
2)
|
chain |
B |
| residue |
630 |
| type |
catalytic |
| sequence |
S
|
| description |
169
|
| source |
MCSA : MCSA2
|
|
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3)
|
chain |
B |
| residue |
631 |
| type |
catalytic |
| sequence |
Y
|
| description |
169
|
| source |
MCSA : MCSA2
|
|
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4)
|
chain |
B |
| residue |
708 |
| type |
catalytic |
| sequence |
D
|
| description |
169
|
| source |
MCSA : MCSA2
|
|
|
5)
|
chain |
B |
| residue |
740 |
| type |
catalytic |
| sequence |
H
|
| description |
169
|
| source |
MCSA : MCSA2
|
|
|
6)
|
chain |
B |
| residue |
630 |
| type |
ACT_SITE |
| sequence |
S
|
| description |
Charge relay system => ECO:0000255|PROSITE-ProRule:PRU10084
|
| source |
Swiss-Prot : SWS_FT_FI1
|
|
|
7)
|
chain |
B |
| residue |
708 |
| type |
ACT_SITE |
| sequence |
D
|
| description |
Charge relay system => ECO:0000255|PROSITE-ProRule:PRU10084
|
| source |
Swiss-Prot : SWS_FT_FI1
|
|
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8)
|
chain |
B |
| residue |
740 |
| type |
ACT_SITE |
| sequence |
H
|
| description |
Charge relay system => ECO:0000255|PROSITE-ProRule:PRU10084
|
| source |
Swiss-Prot : SWS_FT_FI1
|
|
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9)
|
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
|
|
|
10)
|
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
|
|
|
11)
|
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
|
|
|
12)
|
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
|
|
|
13)
|
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
|
|
|
14)
|
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
|
|
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15)
|
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
|
|
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16)
|
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
|
|
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17)
|
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
|
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