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eF-site ID
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1w1i-E |
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PDB Code
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1w1i |
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Chain
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E |
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click to enlarge
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Title
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Crystal structure of dipeptidyl peptidase IV (DPPIV or CD26) in complex with adenosine deaminase |
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Classification
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HYDROLASE |
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Compound
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DIPEPTIDYL PEPTIDASE IV |
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Source
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ORGANISM_COMMON: BOVINE; ORGANISM_SCIENTIFIC: BOS TAURUS; |
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Sequence
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E: |
TPAFDKPKVELHVHLDGAIKPETILYYGKRRGIALPADTP
EELLNIIGMDKPLTLPDFLAKFDYYMPAIAGCRDAIKRIA
YEFVEMKAKDGVVYVEVRYSPHLLANSKVEPIPWNQAEGD
LTPDEVVSLVNQGLQEGERDFGVKVRSILCCMRHQPSWSS
EVVELCKKYREQTVVAIDLAGDETIEGSSLFPGHVQAYAE
AVKSGVHRTVHAGEVGSANVVKEAVDTLKTERLGHGYHTL
EDTTLYNRLRQENMHFEICPWSSYLTGAWKPDTEHAVIRF
KNDQVNYSLNTDDPLIFKSTLDTDYQMTKKDMGFTEEEFK
RLNINAAKSSFLPEDEKKELLDLLYKAYRMPS
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Description
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Functional site
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1)
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chain |
E |
| residue |
16 |
| type |
BINDING |
| sequence |
V
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| 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
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| source |
Swiss-Prot : SWS_FT_FI2
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2)
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chain |
E |
| residue |
18 |
| type |
BINDING |
| sequence |
L
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| 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
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| source |
Swiss-Prot : SWS_FT_FI2
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3)
|
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
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| source |
Swiss-Prot : SWS_FT_FI2
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4)
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chain |
E |
| residue |
296 |
| type |
BINDING |
| sequence |
D
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| 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
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| source |
Swiss-Prot : SWS_FT_FI2
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|
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5)
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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
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| source |
Swiss-Prot : SWS_FT_FI3
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|
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6)
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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
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| source |
Swiss-Prot : SWS_FT_FI4
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7)
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chain |
E |
| residue |
297 |
| type |
BINDING |
| sequence |
P
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| 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
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| source |
Swiss-Prot : SWS_FT_FI5
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8)
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chain |
E |
| residue |
55 |
| type |
MOD_RES |
| sequence |
P
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| description |
N6-acetyllysine => ECO:0000250|UniProtKB:P00813
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| source |
Swiss-Prot : SWS_FT_FI9
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9)
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chain |
E |
| residue |
233 |
| type |
MOD_RES |
| sequence |
T
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| description |
N6-acetyllysine => ECO:0000250|UniProtKB:P00813
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| source |
Swiss-Prot : SWS_FT_FI9
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10)
|
chain |
E |
| residue |
291-297 |
| type |
prosite |
| sequence |
SLNTDDP
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| description |
A_DEAMINASE Adenosine and AMP deaminase signature. SLNTDDP
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| source |
prosite : PS00485
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11)
|
chain |
E |
| residue |
218 |
| type |
ACT_SITE |
| sequence |
V
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| description |
Proton donor => ECO:0000250|UniProtKB:P03958
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| source |
Swiss-Prot : SWS_FT_FI1
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12)
|
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
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| source |
Swiss-Prot : SWS_FT_FI6
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13)
|
chain |
E |
| residue |
63 |
| type |
SITE |
| sequence |
A
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| description |
Important for interaction with adenosine receptors and increasing their affinity for agonists => ECO:0000250|UniProtKB:P00813
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| source |
Swiss-Prot : SWS_FT_FI6
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14)
|
chain |
E |
| residue |
239 |
| type |
SITE |
| sequence |
G
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| description |
Important for catalytic activity => ECO:0000250|UniProtKB:P03958
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| source |
Swiss-Prot : SWS_FT_FI7
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