|
|
eF-site ID
|
1ysb-B |
|
PDB Code
|
1ysb |
|
Chain
|
B |
|
click to enlarge
|
|
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Title
|
Yeast Cytosine Deaminase Triple Mutant |
|
Classification
|
HYDROLASE |
|
Compound
|
Cytosine deaminase |
|
Source
|
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) (FCY1_YEAST) |
|
|
Sequence
|
B: |
GSSMVTGGMASKWDQKGMDIAYEEALLGYKEGGVPIGGCL
INNKDGSVLGRGHNMRFQKGSATLHGEISTLENCGRLEGK
VYKDTTLYTTLSPCDMCTGAIIMYGIPRCVIGENVNFKSK
GEKYLQTRGHEVVVVDDERCKKLMKQFIDERPQDWFEDIG
E
|
|
|
Description
|
|
Functional site
|
|
|
1)
|
chain |
B |
| residue |
262 |
| type |
|
| sequence |
H
|
| description |
BINDING SITE FOR RESIDUE ZN B 500
|
| source |
: AC1
|
|
|
2)
|
chain |
B |
| residue |
291 |
| type |
|
| sequence |
C
|
| description |
BINDING SITE FOR RESIDUE ZN B 500
|
| source |
: AC1
|
|
|
3)
|
chain |
B |
| residue |
294 |
| type |
|
| sequence |
C
|
| description |
BINDING SITE FOR RESIDUE ZN B 500
|
| source |
: AC1
|
|
|
4)
|
chain |
B |
| residue |
264 |
| type |
|
| sequence |
E
|
| description |
BINDING SITE FOR RESIDUE ZN B 502
|
| source |
: AC3
|
|
|
5)
|
chain |
B |
| residue |
326 |
| type |
|
| sequence |
G
|
| description |
BINDING SITE FOR RESIDUE CA B 504
|
| source |
: AC5
|
|
|
6)
|
chain |
B |
| residue |
346 |
| type |
|
| sequence |
D
|
| description |
BINDING SITE FOR RESIDUE CA B 504
|
| source |
: AC5
|
|
|
7)
|
chain |
B |
| residue |
264 |
| type |
ACT_SITE |
| sequence |
E
|
| description |
Proton donor => ECO:0000269|PubMed:12637534, ECO:0007744|PDB:1UAQ
|
| source |
Swiss-Prot : SWS_FT_FI1
|
|
|
8)
|
chain |
B |
| residue |
251 |
| type |
BINDING |
| sequence |
N
|
| description |
BINDING => ECO:0000269|PubMed:12637534, ECO:0000269|PubMed:12906827, ECO:0007744|PDB:1P6O, ECO:0007744|PDB:1UAQ
|
| source |
Swiss-Prot : SWS_FT_FI2
|
|
|
9)
|
chain |
B |
| residue |
355 |
| type |
BINDING |
| sequence |
D
|
| description |
BINDING => ECO:0000269|PubMed:12637534, ECO:0000269|PubMed:12906827, ECO:0007744|PDB:1P6O, ECO:0007744|PDB:1UAQ
|
| source |
Swiss-Prot : SWS_FT_FI2
|
|
|
10)
|
chain |
B |
| residue |
262 |
| type |
catalytic |
| sequence |
H
|
| description |
636
|
| source |
MCSA : MCSA2
|
|
|
11)
|
chain |
B |
| residue |
264 |
| type |
catalytic |
| sequence |
E
|
| description |
636
|
| source |
MCSA : MCSA2
|
|
|
12)
|
chain |
B |
| residue |
289 |
| type |
catalytic |
| sequence |
S
|
| description |
636
|
| source |
MCSA : MCSA2
|
|
|
13)
|
chain |
B |
| residue |
291 |
| type |
catalytic |
| sequence |
C
|
| description |
636
|
| source |
MCSA : MCSA2
|
|
|
14)
|
chain |
B |
| residue |
294 |
| type |
catalytic |
| sequence |
C
|
| description |
636
|
| source |
MCSA : MCSA2
|
|
|
15)
|
chain |
B |
| residue |
262 |
| type |
BINDING |
| sequence |
H
|
| description |
BINDING => ECO:0000269|PubMed:12637534, ECO:0000269|PubMed:12906827, ECO:0000269|PubMed:15879217, ECO:0007744|PDB:1OX7, ECO:0007744|PDB:1P6O, ECO:0007744|PDB:1RB7, ECO:0007744|PDB:1UAQ, ECO:0007744|PDB:1YSB, ECO:0007744|PDB:1YSD
|
| source |
Swiss-Prot : SWS_FT_FI3
|
|
|
16)
|
chain |
B |
| residue |
291 |
| type |
BINDING |
| sequence |
C
|
| description |
BINDING => ECO:0000269|PubMed:12637534, ECO:0000269|PubMed:12906827, ECO:0000269|PubMed:15879217, ECO:0007744|PDB:1OX7, ECO:0007744|PDB:1P6O, ECO:0007744|PDB:1RB7, ECO:0007744|PDB:1UAQ, ECO:0007744|PDB:1YSB, ECO:0007744|PDB:1YSD
|
| source |
Swiss-Prot : SWS_FT_FI3
|
|
|
17)
|
chain |
B |
| residue |
294 |
| type |
BINDING |
| sequence |
C
|
| description |
BINDING => ECO:0000269|PubMed:12637534, ECO:0000269|PubMed:12906827, ECO:0000269|PubMed:15879217, ECO:0007744|PDB:1OX7, ECO:0007744|PDB:1P6O, ECO:0007744|PDB:1RB7, ECO:0007744|PDB:1UAQ, ECO:0007744|PDB:1YSB, ECO:0007744|PDB:1YSD
|
| source |
Swiss-Prot : SWS_FT_FI3
|
|
|
|