|
|
eF-site ID
|
1w1i-ABEF |
|
PDB Code
|
1w1i |
|
Chain
|
A, B, E, F |
|
click to enlarge
|
|
|
Title
|
Crystal structure of dipeptidyl peptidase IV (DPPIV or CD26) in complex with adenosine deaminase |
|
Classification
|
HYDROLASE |
|
Compound
|
DIPEPTIDYL PEPTIDASE IV |
|
Source
|
ORGANISM_COMMON: BOVINE; ORGANISM_SCIENTIFIC: BOS TAURUS; |
|
|
Sequence
|
A: |
SRKTYTLTDYLKNTYRLKLYSLRWISDHEYLYKQENNILV
FNAEYGNSSVFLENSTFDEFGHSINDYSISPDGQFILLEY
NYVKQWRHSYTASYDIYDLNKRQLITEERIPNNTQWVTWS
PVGHKLAYVWNNDIYVKIEPNLPSYRITWTGKEDIIYNGI
TDWVYEEEVFSAYSALWWSPNGTFLAYAQFNDTEVPLIEY
SFYSDESLQYPKTVRVPYPKAGAVNPTVKFFVVNTDSLSS
VTNATSIQITAPASMLIGDHYLCDVTWATQERISLQWLRR
IQNYSVMDICDYDESSGRWNCLVARQHIEMSTTGWVGRFR
PSEPHFTLDGNSFYKIISNEEGYRHICYFQIDKKDCTFIT
KGTWEVIGIEALTSDYLYYISNEYKGMPGGRNLYKIQLSD
YTKVTCLSCELNPERCQYYSVSFSKEAKYYQLRCSGPGLP
LYTLHSSVNDKGLRVLEDNSALDKMLQNVQMPSKKLDFII
LNETKFWYQMILPPHFDKSKKYPLLLDVYAGPCSQKADTV
FRLNWATYLASTENIIVASFDGRGSGYQGDKIMHAINRRL
GTFEVEDQIEAARQFSKMGFVDNKRIAIWGWSYGGYVTSM
VLGSGSGVFKCGIAVAPVSRWEYYDSVYTERYMGLPTPED
NLDHYRNSTVMSRAENFKQVEYLLIHGTADDNVHFQQSAQ
ISKALVDVGVDFQAMWYTDEDHGIASSTAHQHIYTHMSHF
IKQCFSLP
|
| B: |
SRKTYTLTDYLKNTYRLKLYSLRWISDHEYLYKQENNILV
FNAEYGNSSVFLENSTFDEFGHSINDYSISPDGQFILLEY
NYVKQWRHSYTASYDIYDLNKRQLITEERIPNNTQWVTWS
PVGHKLAYVWNNDIYVKIEPNLPSYRITWTGKEDIIYNGI
TDWVYEEEVFSAYSALWWSPNGTFLAYAQFNDTEVPLIEY
SFYSDESLQYPKTVRVPYPKAGAVNPTVKFFVVNTDSLSS
VTNATSIQITAPASMLIGDHYLCDVTWATQERISLQWLRR
IQNYSVMDICDYDESSGRWNCLVARQHIEMSTTGWVGRFR
PSEPHFTLDGNSFYKIISNEEGYRHICYFQIDKKDCTFIT
KGTWEVIGIEALTSDYLYYISNEYKGMPGGRNLYKIQLSD
YTKVTCLSCELNPERCQYYSVSFSKEAKYYQLRCSGPGLP
LYTLHSSVNDKGLRVLEDNSALDKMLQNVQMPSKKLDFII
LNETKFWYQMILPPHFDKSKKYPLLLDVYAGPCSQKADTV
FRLNWATYLASTENIIVASFDGRGSGYQGDKIMHAINRRL
GTFEVEDQIEAARQFSKMGFVDNKRIAIWGWSYGGYVTSM
VLGSGSGVFKCGIAVAPVSRWEYYDSVYTERYMGLPTPED
NLDHYRNSTVMSRAENFKQVEYLLIHGTADDNVHFQQSAQ
ISKALVDVGVDFQAMWYTDEDHGIASSTAHQHIYTHMSHF
IKQCFSLP
|
| E: |
TPAFDKPKVELHVHLDGAIKPETILYYGKRRGIALPADTP
EELLNIIGMDKPLTLPDFLAKFDYYMPAIAGCRDAIKRIA
YEFVEMKAKDGVVYVEVRYSPHLLANSKVEPIPWNQAEGD
LTPDEVVSLVNQGLQEGERDFGVKVRSILCCMRHQPSWSS
EVVELCKKYREQTVVAIDLAGDETIEGSSLFPGHVQAYAE
AVKSGVHRTVHAGEVGSANVVKEAVDTLKTERLGHGYHTL
EDTTLYNRLRQENMHFEICPWSSYLTGAWKPDTEHAVIRF
KNDQVNYSLNTDDPLIFKSTLDTDYQMTKKDMGFTEEEFK
RLNINAAKSSFLPEDEKKELLDLLYKAYRMPS
|
| F: |
TPAFDKPKVELHVHLDGAIKPETILYYGKRRGIALPADTP
EELLNIIGMDKPLTLPDFLAKFDYYMPAIAGCRDAIKRIA
YEFVEMKAKDGVVYVEVRYSPHLLANSKVEPIPWNQAEGD
LTPDEVVSLVNQGLQEGERDFGVKVRSILCCMRHQPSWSS
EVVELCKKYREQTVVAIDLAGDETIEGSSLFPGHVQAYAE
AVKSGVHRTVHAGEVGSANVVKEAVDTLKTERLGHGYHTL
EDTTLYNRLRQENMHFEICPWSSYLTGAWKPDTEHAVIRF
KNDQVNYSLNTDDPLIFKSTLDTDYQMTKKDMGFTEEEFK
RLNINAAKSSFLPEDEKKELLDLLYKAYRMPS
|
|
|
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 |
B |
| residue |
547 |
| type |
catalytic |
| sequence |
Y
|
| description |
169
|
| source |
MCSA : MCSA2
|
|
|
7)
|
chain |
B |
| residue |
630 |
| type |
catalytic |
| sequence |
S
|
| description |
169
|
| source |
MCSA : MCSA2
|
|
|
8)
|
chain |
B |
| residue |
631 |
| type |
catalytic |
| sequence |
Y
|
| description |
169
|
| source |
MCSA : MCSA2
|
|
|
9)
|
chain |
B |
| residue |
708 |
| type |
catalytic |
| sequence |
D
|
| description |
169
|
| source |
MCSA : MCSA2
|
|
|
10)
|
chain |
B |
| residue |
740 |
| type |
catalytic |
| sequence |
H
|
| description |
169
|
| source |
MCSA : MCSA2
|
|
|
11)
|
chain |
E |
| residue |
16 |
| type |
BINDING |
| sequence |
V
|
| description |
BINDING => ECO:0000269|PubMed:12554940, ECO:0000269|PubMed:14709046, ECO:0000269|PubMed:15139750, ECO:0000269|PubMed:15213224, ECO:0000269|PubMed:15239652, ECO:0000269|PubMed:15695814, ECO:0000269|PubMed:16033254, ECO:0000269|PubMed:16060665, ECO:0000269|PubMed:18549808, ECO:0007744|PDB:1KRM, ECO:0007744|PDB:1NDV, ECO:0007744|PDB:1NDW, ECO:0007744|PDB:1NDY, ECO:0007744|PDB:1NDZ, ECO:0007744|PDB:1O5R, ECO:0007744|PDB:1QXL, ECO:0007744|PDB:1VFL
|
| source |
Swiss-Prot : SWS_FT_FI2
|
|
|
12)
|
chain |
E |
| residue |
18 |
| type |
BINDING |
| sequence |
L
|
| description |
BINDING => ECO:0000269|PubMed:12554940, ECO:0000269|PubMed:14709046, ECO:0000269|PubMed:15139750, ECO:0000269|PubMed:15213224, ECO:0000269|PubMed:15239652, ECO:0000269|PubMed:15695814, ECO:0000269|PubMed:16033254, ECO:0000269|PubMed:16060665, ECO:0000269|PubMed:18549808, ECO:0007744|PDB:1KRM, ECO:0007744|PDB:1NDV, ECO:0007744|PDB:1NDW, ECO:0007744|PDB:1NDY, ECO:0007744|PDB:1NDZ, ECO:0007744|PDB:1O5R, ECO:0007744|PDB:1QXL, ECO:0007744|PDB:1VFL
|
| source |
Swiss-Prot : SWS_FT_FI2
|
|
|
13)
|
chain |
E |
| residue |
215 |
| type |
BINDING |
| sequence |
A
|
| description |
BINDING => ECO:0000269|PubMed:12554940, ECO:0000269|PubMed:14709046, ECO:0000269|PubMed:15139750, ECO:0000269|PubMed:15213224, ECO:0000269|PubMed:15239652, ECO:0000269|PubMed:15695814, ECO:0000269|PubMed:16033254, ECO:0000269|PubMed:16060665, ECO:0000269|PubMed:18549808, ECO:0007744|PDB:1KRM, ECO:0007744|PDB:1NDV, ECO:0007744|PDB:1NDW, ECO:0007744|PDB:1NDY, ECO:0007744|PDB:1NDZ, ECO:0007744|PDB:1O5R, ECO:0007744|PDB:1QXL, ECO:0007744|PDB:1VFL
|
| source |
Swiss-Prot : SWS_FT_FI2
|
|
|
14)
|
chain |
E |
| residue |
296 |
| type |
BINDING |
| sequence |
D
|
| description |
BINDING => ECO:0000269|PubMed:12554940, ECO:0000269|PubMed:14709046, ECO:0000269|PubMed:15139750, ECO:0000269|PubMed:15213224, ECO:0000269|PubMed:15239652, ECO:0000269|PubMed:15695814, ECO:0000269|PubMed:16033254, ECO:0000269|PubMed:16060665, ECO:0000269|PubMed:18549808, ECO:0007744|PDB:1KRM, ECO:0007744|PDB:1NDV, ECO:0007744|PDB:1NDW, ECO:0007744|PDB:1NDY, ECO:0007744|PDB:1NDZ, ECO:0007744|PDB:1O5R, ECO:0007744|PDB:1QXL, ECO:0007744|PDB:1VFL
|
| source |
Swiss-Prot : SWS_FT_FI2
|
|
|
15)
|
chain |
F |
| residue |
16 |
| type |
BINDING |
| sequence |
V
|
| description |
BINDING => ECO:0000269|PubMed:12554940, ECO:0000269|PubMed:14709046, ECO:0000269|PubMed:15139750, ECO:0000269|PubMed:15213224, ECO:0000269|PubMed:15239652, ECO:0000269|PubMed:15695814, ECO:0000269|PubMed:16033254, ECO:0000269|PubMed:16060665, ECO:0000269|PubMed:18549808, ECO:0007744|PDB:1KRM, ECO:0007744|PDB:1NDV, ECO:0007744|PDB:1NDW, ECO:0007744|PDB:1NDY, ECO:0007744|PDB:1NDZ, ECO:0007744|PDB:1O5R, ECO:0007744|PDB:1QXL, ECO:0007744|PDB:1VFL
|
| source |
Swiss-Prot : SWS_FT_FI2
|
|
|
16)
|
chain |
F |
| residue |
18 |
| type |
BINDING |
| sequence |
L
|
| description |
BINDING => ECO:0000269|PubMed:12554940, ECO:0000269|PubMed:14709046, ECO:0000269|PubMed:15139750, ECO:0000269|PubMed:15213224, ECO:0000269|PubMed:15239652, ECO:0000269|PubMed:15695814, ECO:0000269|PubMed:16033254, ECO:0000269|PubMed:16060665, ECO:0000269|PubMed:18549808, ECO:0007744|PDB:1KRM, ECO:0007744|PDB:1NDV, ECO:0007744|PDB:1NDW, ECO:0007744|PDB:1NDY, ECO:0007744|PDB:1NDZ, ECO:0007744|PDB:1O5R, ECO:0007744|PDB:1QXL, ECO:0007744|PDB:1VFL
|
| source |
Swiss-Prot : SWS_FT_FI2
|
|
|
17)
|
chain |
F |
| residue |
215 |
| type |
BINDING |
| sequence |
A
|
| description |
BINDING => ECO:0000269|PubMed:12554940, ECO:0000269|PubMed:14709046, ECO:0000269|PubMed:15139750, ECO:0000269|PubMed:15213224, ECO:0000269|PubMed:15239652, ECO:0000269|PubMed:15695814, ECO:0000269|PubMed:16033254, ECO:0000269|PubMed:16060665, ECO:0000269|PubMed:18549808, ECO:0007744|PDB:1KRM, ECO:0007744|PDB:1NDV, ECO:0007744|PDB:1NDW, ECO:0007744|PDB:1NDY, ECO:0007744|PDB:1NDZ, ECO:0007744|PDB:1O5R, ECO:0007744|PDB:1QXL, ECO:0007744|PDB:1VFL
|
| source |
Swiss-Prot : SWS_FT_FI2
|
|
|
18)
|
chain |
F |
| residue |
296 |
| type |
BINDING |
| sequence |
D
|
| description |
BINDING => ECO:0000269|PubMed:12554940, ECO:0000269|PubMed:14709046, ECO:0000269|PubMed:15139750, ECO:0000269|PubMed:15213224, ECO:0000269|PubMed:15239652, ECO:0000269|PubMed:15695814, ECO:0000269|PubMed:16033254, ECO:0000269|PubMed:16060665, ECO:0000269|PubMed:18549808, ECO:0007744|PDB:1KRM, ECO:0007744|PDB:1NDV, ECO:0007744|PDB:1NDW, ECO:0007744|PDB:1NDY, ECO:0007744|PDB:1NDZ, ECO:0007744|PDB:1O5R, ECO:0007744|PDB:1QXL, ECO:0007744|PDB:1VFL
|
| source |
Swiss-Prot : SWS_FT_FI2
|
|
|
19)
|
chain |
E |
| residue |
20 |
| type |
BINDING |
| sequence |
G
|
| description |
BINDING => ECO:0000269|PubMed:12554940, ECO:0000269|PubMed:14709046, ECO:0000269|PubMed:15139750, ECO:0000269|PubMed:15239652, ECO:0000269|PubMed:16033254, ECO:0000269|PubMed:16060665, ECO:0000269|PubMed:18549808, ECO:0007744|PDB:1NDW, ECO:0007744|PDB:1NDY, ECO:0007744|PDB:1NDZ, ECO:0007744|PDB:1O5R, ECO:0007744|PDB:1QXL
|
| source |
Swiss-Prot : SWS_FT_FI3
|
|
|
20)
|
chain |
F |
| residue |
20 |
| type |
BINDING |
| sequence |
G
|
| description |
BINDING => ECO:0000269|PubMed:12554940, ECO:0000269|PubMed:14709046, ECO:0000269|PubMed:15139750, ECO:0000269|PubMed:15239652, ECO:0000269|PubMed:16033254, ECO:0000269|PubMed:16060665, ECO:0000269|PubMed:18549808, ECO:0007744|PDB:1NDW, ECO:0007744|PDB:1NDY, ECO:0007744|PDB:1NDZ, ECO:0007744|PDB:1O5R, ECO:0007744|PDB:1QXL
|
| source |
Swiss-Prot : SWS_FT_FI3
|
|
|
21)
|
chain |
E |
| residue |
185 |
| type |
BINDING |
| sequence |
D
|
| description |
BINDING => ECO:0000269|PubMed:14709046, ECO:0000269|PubMed:16060665, ECO:0007744|PDB:1NDY, ECO:0007744|PDB:1WXY
|
| source |
Swiss-Prot : SWS_FT_FI4
|
|
|
22)
|
chain |
F |
| residue |
185 |
| type |
BINDING |
| sequence |
D
|
| description |
BINDING => ECO:0000269|PubMed:14709046, ECO:0000269|PubMed:16060665, ECO:0007744|PDB:1NDY, ECO:0007744|PDB:1WXY
|
| source |
Swiss-Prot : SWS_FT_FI4
|
|
|
23)
|
chain |
E |
| residue |
297 |
| type |
BINDING |
| sequence |
P
|
| description |
BINDING => ECO:0000269|PubMed:12554940, ECO:0000269|PubMed:14709046, ECO:0000269|PubMed:15139750, ECO:0000269|PubMed:15239652, ECO:0000269|PubMed:16033254, ECO:0000269|PubMed:18549808, ECO:0007744|PDB:1NDW, ECO:0007744|PDB:1NDY, ECO:0007744|PDB:1NDZ, ECO:0007744|PDB:1O5R, ECO:0007744|PDB:1QXL
|
| source |
Swiss-Prot : SWS_FT_FI5
|
|
|
24)
|
chain |
F |
| residue |
297 |
| type |
BINDING |
| sequence |
P
|
| description |
BINDING => ECO:0000269|PubMed:12554940, ECO:0000269|PubMed:14709046, ECO:0000269|PubMed:15139750, ECO:0000269|PubMed:15239652, ECO:0000269|PubMed:16033254, ECO:0000269|PubMed:18549808, ECO:0007744|PDB:1NDW, ECO:0007744|PDB:1NDY, ECO:0007744|PDB:1NDZ, ECO:0007744|PDB:1O5R, ECO:0007744|PDB:1QXL
|
| source |
Swiss-Prot : SWS_FT_FI5
|
|
|
25)
|
chain |
E |
| residue |
55 |
| type |
MOD_RES |
| sequence |
P
|
| description |
N6-acetyllysine => ECO:0000250|UniProtKB:P00813
|
| source |
Swiss-Prot : SWS_FT_FI9
|
|
|
26)
|
chain |
E |
| residue |
233 |
| type |
MOD_RES |
| sequence |
T
|
| description |
N6-acetyllysine => ECO:0000250|UniProtKB:P00813
|
| source |
Swiss-Prot : SWS_FT_FI9
|
|
|
27)
|
chain |
F |
| residue |
55 |
| type |
MOD_RES |
| sequence |
P
|
| description |
N6-acetyllysine => ECO:0000250|UniProtKB:P00813
|
| source |
Swiss-Prot : SWS_FT_FI9
|
|
|
28)
|
chain |
F |
| residue |
233 |
| type |
MOD_RES |
| sequence |
T
|
| description |
N6-acetyllysine => ECO:0000250|UniProtKB:P00813
|
| source |
Swiss-Prot : SWS_FT_FI9
|
|
|
29)
|
chain |
A |
| residue |
605-635 |
| type |
prosite |
| sequence |
DQIEAARQFSKMGFVDNKRIAIWGWSYGGYV
|
| description |
PRO_ENDOPEP_SER Prolyl endopeptidase family serine active site. DqieAarqFskmgfvdnkriaiwGwSyGGYV
|
| source |
prosite : PS00708
|
|
|
30)
|
chain |
E |
| residue |
291-297 |
| type |
prosite |
| sequence |
SLNTDDP
|
| description |
A_DEAMINASE Adenosine and AMP deaminase signature. SLNTDDP
|
| source |
prosite : PS00485
|
|
|
31)
|
chain |
E |
| residue |
218 |
| type |
ACT_SITE |
| sequence |
V
|
| description |
Proton donor => ECO:0000250|UniProtKB:P03958
|
| source |
Swiss-Prot : SWS_FT_FI1
|
|
|
32)
|
chain |
F |
| residue |
218 |
| type |
ACT_SITE |
| sequence |
V
|
| description |
Proton donor => ECO:0000250|UniProtKB:P03958
|
| source |
Swiss-Prot : SWS_FT_FI1
|
|
|
33)
|
chain |
B |
| residue |
708 |
| type |
ACT_SITE |
| sequence |
D
|
| description |
Proton donor => ECO:0000250|UniProtKB:P03958
|
| source |
Swiss-Prot : SWS_FT_FI1
|
|
|
34)
|
chain |
B |
| residue |
740 |
| type |
ACT_SITE |
| sequence |
H
|
| description |
Proton donor => ECO:0000250|UniProtKB:P03958
|
| source |
Swiss-Prot : SWS_FT_FI1
|
|
|
35)
|
chain |
E |
| residue |
59 |
| type |
SITE |
| sequence |
P
|
| description |
Important for interaction with adenosine receptors and increasing their affinity for agonists => ECO:0000250|UniProtKB:P00813
|
| source |
Swiss-Prot : SWS_FT_FI6
|
|
|
36)
|
chain |
E |
| residue |
63 |
| type |
SITE |
| sequence |
A
|
| description |
Important for interaction with adenosine receptors and increasing their affinity for agonists => ECO:0000250|UniProtKB:P00813
|
| source |
Swiss-Prot : SWS_FT_FI6
|
|
|
37)
|
chain |
F |
| residue |
59 |
| type |
SITE |
| sequence |
P
|
| description |
Important for interaction with adenosine receptors and increasing their affinity for agonists => ECO:0000250|UniProtKB:P00813
|
| source |
Swiss-Prot : SWS_FT_FI6
|
|
|
38)
|
chain |
F |
| residue |
63 |
| type |
SITE |
| sequence |
A
|
| description |
Important for interaction with adenosine receptors and increasing their affinity for agonists => ECO:0000250|UniProtKB:P00813
|
| source |
Swiss-Prot : SWS_FT_FI6
|
|
|
39)
|
chain |
E |
| residue |
239 |
| type |
SITE |
| sequence |
G
|
| description |
Important for catalytic activity => ECO:0000250|UniProtKB:P03958
|
| source |
Swiss-Prot : SWS_FT_FI7
|
|
|
40)
|
chain |
F |
| residue |
239 |
| type |
SITE |
| sequence |
G
|
| description |
Important for catalytic activity => ECO:0000250|UniProtKB:P03958
|
| source |
Swiss-Prot : SWS_FT_FI7
|
|
|
|