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eF-site ID
|
4tti-B |
|
PDB Code
|
4tti |
|
Chain
|
B |
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click to enlarge
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Title
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Crystal structure of double mutant E. Coli purine nucleoside phosphorylase with 4 FMC molecules |
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Classification
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TRANSFERASE |
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Compound
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Purine nucleoside phosphorylase DeoD-type |
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Source
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(DEOD_ECOLI) |
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Sequence
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B: |
ATPHINAEMGDFADVVLMPGDPLRAKYIAETFLEDAREVN
NVRGMLGFTGTYKGRKISVMGHGMGIPSCSIYTKELITDF
GVKKIIRVGSCGAVLPHVKLRDVVIGMGACTDSKVNRIRF
KDHDFAAIADFDMVRNAVDAAKALGIDARVGNLFSADLFY
SPDGEMFDVMEKYGILGVEMEAAGIYGVAAEFGAKALTIC
TVSAHIRTHEQTTAAEAQTTFNDMIKIALESVLLGDK
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Description
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Functional site
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|
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1)
|
chain |
B |
| residue |
20 |
| type |
|
| sequence |
G
|
| description |
binding site for residue PO4 B 301
|
| source |
: AC3
|
|
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2)
|
chain |
B |
| residue |
24 |
| type |
|
| sequence |
R
|
| description |
binding site for residue PO4 B 301
|
| source |
: AC3
|
|
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3)
|
chain |
B |
| residue |
87 |
| type |
|
| sequence |
R
|
| description |
binding site for residue PO4 B 301
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| source |
: AC3
|
|
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4)
|
chain |
B |
| residue |
89 |
| type |
|
| sequence |
G
|
| description |
binding site for residue PO4 B 301
|
| source |
: AC3
|
|
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5)
|
chain |
B |
| residue |
90 |
| type |
|
| sequence |
S
|
| description |
binding site for residue PO4 B 301
|
| source |
: AC3
|
|
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6)
|
chain |
B |
| residue |
43 |
| type |
|
| sequence |
R
|
| description |
binding site for residue PO4 E 301
|
| source |
: AD2
|
|
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7)
|
chain |
B |
| residue |
43 |
| type |
BINDING |
| sequence |
R
|
| description |
BINDING => ECO:0000269|PubMed:11786017, ECO:0000269|PubMed:21672603, ECO:0000269|PubMed:30337572, ECO:0007744|PDB:1K9S, ECO:0007744|PDB:3ONV, ECO:0007744|PDB:3OOE, ECO:0007744|PDB:3OOH, ECO:0007744|PDB:3OPV, ECO:0007744|PDB:4TS3, ECO:0007744|PDB:4TS9, ECO:0007744|PDB:4TTA, ECO:0007744|PDB:4TTI, ECO:0007744|PDB:4TTJ
|
| source |
Swiss-Prot : SWS_FT_FI4
|
|
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8)
|
chain |
B |
| residue |
179 |
| type |
BINDING |
| sequence |
E
|
| description |
in other chain => ECO:0000305|PubMed:30337572, ECO:0007744|PDB:4TS3, ECO:0007744|PDB:4TS9, ECO:0007744|PDB:4TTA, ECO:0007744|PDB:4TTI, ECO:0007744|PDB:4TTJ
|
| source |
Swiss-Prot : SWS_FT_FI5
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|
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9)
|
chain |
B |
| residue |
203 |
| type |
BINDING |
| sequence |
S
|
| description |
in other chain => ECO:0000305|PubMed:30337572, ECO:0007744|PDB:4TS3, ECO:0007744|PDB:4TS9, ECO:0007744|PDB:4TTA, ECO:0007744|PDB:4TTI, ECO:0007744|PDB:4TTJ
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| source |
Swiss-Prot : SWS_FT_FI5
|
|
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10)
|
chain |
B |
| residue |
20 |
| type |
catalytic |
| sequence |
G
|
| description |
375
|
| source |
MCSA : MCSA2
|
|
|
11)
|
chain |
B |
| residue |
24 |
| type |
catalytic |
| sequence |
R
|
| description |
375
|
| source |
MCSA : MCSA2
|
|
|
12)
|
chain |
B |
| residue |
43 |
| type |
catalytic |
| sequence |
R
|
| description |
375
|
| source |
MCSA : MCSA2
|
|
|
13)
|
chain |
B |
| residue |
87 |
| type |
catalytic |
| sequence |
R
|
| description |
375
|
| source |
MCSA : MCSA2
|
|
|
14)
|
chain |
B |
| residue |
90 |
| type |
catalytic |
| sequence |
S
|
| description |
375
|
| source |
MCSA : MCSA2
|
|
|
15)
|
chain |
B |
| residue |
204 |
| type |
catalytic |
| sequence |
A
|
| description |
375
|
| source |
MCSA : MCSA2
|
|
|
16)
|
chain |
B |
| residue |
217 |
| type |
catalytic |
| sequence |
A
|
| description |
375
|
| source |
MCSA : MCSA2
|
|
|
17)
|
chain |
B |
| residue |
204 |
| type |
ACT_SITE |
| sequence |
A
|
| description |
Proton donor => ECO:0000255|HAMAP-Rule:MF_01627, ECO:0000269|PubMed:30337572
|
| source |
Swiss-Prot : SWS_FT_FI1
|
|
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18)
|
chain |
B |
| residue |
217 |
| type |
SITE |
| sequence |
A
|
| description |
Important for catalytic activity => ECO:0000255|HAMAP-Rule:MF_01627, ECO:0000269|PubMed:21672603, ECO:0000269|PubMed:30337572
|
| source |
Swiss-Prot : SWS_FT_FI6
|
|
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19)
|
chain |
B |
| residue |
26 |
| type |
MOD_RES |
| sequence |
K
|
| description |
N6-acetyllysine => ECO:0000269|PubMed:18723842
|
| source |
Swiss-Prot : SWS_FT_FI7
|
|
|
20)
|
chain |
B |
| residue |
4 |
| type |
BINDING |
| sequence |
H
|
| description |
BINDING => ECO:0000305|PubMed:30337572, ECO:0007744|PDB:4TS3, ECO:0007744|PDB:4TS9, ECO:0007744|PDB:4TTA, ECO:0007744|PDB:4TTI, ECO:0007744|PDB:4TTJ
|
| source |
Swiss-Prot : SWS_FT_FI2
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|
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21)
|
chain |
B |
| residue |
20 |
| type |
BINDING |
| sequence |
G
|
| description |
in other chain => ECO:0000269|PubMed:11786017, ECO:0000269|PubMed:21672603, ECO:0000269|PubMed:30337572, ECO:0007744|PDB:1K9S, ECO:0007744|PDB:3ONV, ECO:0007744|PDB:3OOE, ECO:0007744|PDB:3OOH, ECO:0007744|PDB:3OPV, ECO:0007744|PDB:4TS3, ECO:0007744|PDB:4TS9, ECO:0007744|PDB:4TTA, ECO:0007744|PDB:4TTI, ECO:0007744|PDB:4TTJ
|
| source |
Swiss-Prot : SWS_FT_FI3
|
|
|
22)
|
chain |
B |
| residue |
24 |
| type |
BINDING |
| sequence |
R
|
| description |
in other chain => ECO:0000269|PubMed:11786017, ECO:0000269|PubMed:21672603, ECO:0000269|PubMed:30337572, ECO:0007744|PDB:1K9S, ECO:0007744|PDB:3ONV, ECO:0007744|PDB:3OOE, ECO:0007744|PDB:3OOH, ECO:0007744|PDB:3OPV, ECO:0007744|PDB:4TS3, ECO:0007744|PDB:4TS9, ECO:0007744|PDB:4TTA, ECO:0007744|PDB:4TTI, ECO:0007744|PDB:4TTJ
|
| source |
Swiss-Prot : SWS_FT_FI3
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|
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23)
|
chain |
B |
| residue |
87 |
| type |
BINDING |
| sequence |
R
|
| description |
in other chain => ECO:0000269|PubMed:11786017, ECO:0000269|PubMed:21672603, ECO:0000269|PubMed:30337572, ECO:0007744|PDB:1K9S, ECO:0007744|PDB:3ONV, ECO:0007744|PDB:3OOE, ECO:0007744|PDB:3OOH, ECO:0007744|PDB:3OPV, ECO:0007744|PDB:4TS3, ECO:0007744|PDB:4TS9, ECO:0007744|PDB:4TTA, ECO:0007744|PDB:4TTI, ECO:0007744|PDB:4TTJ
|
| source |
Swiss-Prot : SWS_FT_FI3
|
|
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