|
|
eF-site ID
|
1cvd-A |
|
PDB Code
|
1cvd |
|
Chain
|
A |
|
click to enlarge
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Title
|
STRUCTURAL CONSEQUENCES OF REDESIGNING A PROTEIN-ZINC BINDING SITE |
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Classification
|
LYASE(OXO-ACID) |
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Compound
|
CARBONIC ANHYDRASE II |
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Source
|
null (CAH2_HUMAN) |
|
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Sequence
|
A: |
WGYGKHNGPEHWHKDFPIAKGERQSPVDIDTHTAKYDPSL
KPLSVSYDQATSLRILNNGHAFNVEFDDSQDKAVLKGGPL
DGTYRLIQFHFHWGSLDGQGSEHTVDKKKYAAELCLVHWN
TKYGDFGKAVQQPDGLAVLGIFLKVGSAKPGLQKVVDVLD
SIKTKGKSADFTNFDPRGLLPESLDYWTYPGSLTTPPLLE
CVTWIVLKEPISVSSEQVLKFRKLNFNGEGEPEELMVDNW
RPAQPLKNRQIKASF
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|
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Description
|
|
Functional site
|
|
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1)
|
chain |
A |
| residue |
94 |
| type |
|
| sequence |
H
|
| description |
BINDING SITE FOR RESIDUE ZN A 262
|
| source |
: AC1
|
|
|
2)
|
chain |
A |
| residue |
96 |
| type |
|
| sequence |
H
|
| description |
BINDING SITE FOR RESIDUE ZN A 262
|
| source |
: AC1
|
|
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3)
|
chain |
A |
| residue |
119 |
| type |
|
| sequence |
C
|
| description |
BINDING SITE FOR RESIDUE ZN A 262
|
| source |
: AC1
|
|
|
4)
|
chain |
A |
| residue |
65 |
| type |
catalytic |
| sequence |
A
|
| description |
216
|
| source |
MCSA : MCSA1
|
|
|
5)
|
chain |
A |
| residue |
95 |
| type |
catalytic |
| sequence |
F
|
| description |
216
|
| source |
MCSA : MCSA1
|
|
|
6)
|
chain |
A |
| residue |
97 |
| type |
catalytic |
| sequence |
W
|
| description |
216
|
| source |
MCSA : MCSA1
|
|
|
7)
|
chain |
A |
| residue |
107 |
| type |
catalytic |
| sequence |
H
|
| description |
216
|
| source |
MCSA : MCSA1
|
|
|
8)
|
chain |
A |
| residue |
120 |
| type |
catalytic |
| sequence |
L
|
| description |
216
|
| source |
MCSA : MCSA1
|
|
|
9)
|
chain |
A |
| residue |
200 |
| type |
catalytic |
| sequence |
T
|
| description |
216
|
| source |
MCSA : MCSA1
|
|
|
10)
|
chain |
A |
| residue |
93 |
| type |
SITE |
| sequence |
F
|
| description |
Involved in the binding of some activators, including histamine and L-histidine => ECO:0000269|PubMed:16214338, ECO:0000269|PubMed:9265618, ECO:0000305|PubMed:17330962
|
| source |
Swiss-Prot : SWS_FT_FI7
|
|
|
11)
|
chain |
A |
| residue |
65 |
| type |
ACT_SITE |
| sequence |
A
|
| description |
Proton donor/acceptor => ECO:0000305|PubMed:15667203, ECO:0000305|PubMed:17330962
|
| source |
Swiss-Prot : SWS_FT_FI1
|
|
|
12)
|
chain |
A |
| residue |
95 |
| type |
BINDING |
| sequence |
F
|
| description |
BINDING => ECO:0000269|PubMed:11076507, ECO:0000269|PubMed:12499545, ECO:0000269|PubMed:1336460, ECO:0000269|PubMed:1433293, ECO:0000269|PubMed:1909891, ECO:0000269|PubMed:19583303, ECO:0000269|PubMed:3151019, ECO:0000269|PubMed:3151020, ECO:0000269|PubMed:4621826, ECO:0000269|PubMed:7761440, ECO:0000269|PubMed:7803386, ECO:0000269|PubMed:7901850, ECO:0000269|PubMed:8218160, ECO:0000269|PubMed:8262987, ECO:0000269|PubMed:8331673, ECO:0000269|PubMed:8399159, ECO:0000269|PubMed:8431430, ECO:0000269|PubMed:8451242, ECO:0000269|PubMed:8482389, ECO:0000269|PubMed:8639494, ECO:0000269|PubMed:8987974, ECO:0000269|PubMed:9398308, ECO:0000269|PubMed:9865942
|
| source |
Swiss-Prot : SWS_FT_FI2
|
|
|
13)
|
chain |
A |
| residue |
200 |
| type |
BINDING |
| sequence |
T
|
| description |
BINDING => ECO:0000269|PubMed:10550681, ECO:0000269|PubMed:19520834
|
| source |
Swiss-Prot : SWS_FT_FI4
|
|
|
14)
|
chain |
A |
| residue |
8 |
| type |
SITE |
| sequence |
G
|
| description |
Fine-tunes the proton-transfer properties of H-64 => ECO:0000305|PubMed:17330962
|
| source |
Swiss-Prot : SWS_FT_FI5
|
|
|
15)
|
chain |
A |
| residue |
167 |
| type |
MOD_RES |
| sequence |
I
|
| description |
Phosphoserine => ECO:0007744|PubMed:24275569
|
| source |
Swiss-Prot : SWS_FT_FI8
|
|
|
16)
|
chain |
A |
| residue |
174 |
| type |
MOD_RES |
| sequence |
A
|
| description |
Phosphoserine => ECO:0007744|PubMed:24275569
|
| source |
Swiss-Prot : SWS_FT_FI8
|
|
|
17)
|
chain |
A |
| residue |
120 |
| type |
BINDING |
| sequence |
L
|
| description |
BINDING => ECO:0000269|PubMed:11076507, ECO:0000269|PubMed:12499545, ECO:0000269|PubMed:1336460, ECO:0000269|PubMed:1433293, ECO:0000269|PubMed:1909891, ECO:0000269|PubMed:19583303, ECO:0000269|PubMed:3151019, ECO:0000269|PubMed:3151020, ECO:0000269|PubMed:7761440, ECO:0000269|PubMed:7803386, ECO:0000269|PubMed:7901850, ECO:0000269|PubMed:8218160, ECO:0000269|PubMed:8262987, ECO:0000269|PubMed:8331673, ECO:0000269|PubMed:8399159, ECO:0000269|PubMed:8431430, ECO:0000269|PubMed:8451242, ECO:0000269|PubMed:8482389, ECO:0000269|PubMed:8639494, ECO:0000269|PubMed:8987974, ECO:0000269|PubMed:9398308, ECO:0000269|PubMed:9865942
|
| source |
Swiss-Prot : SWS_FT_FI3
|
|
|
18)
|
chain |
A |
| residue |
97 |
| type |
BINDING |
| sequence |
W
|
| description |
BINDING => ECO:0000269|PubMed:11076507, ECO:0000269|PubMed:12499545, ECO:0000269|PubMed:1336460, ECO:0000269|PubMed:1433293, ECO:0000269|PubMed:1909891, ECO:0000269|PubMed:19583303, ECO:0000269|PubMed:3151019, ECO:0000269|PubMed:3151020, ECO:0000269|PubMed:7761440, ECO:0000269|PubMed:7803386, ECO:0000269|PubMed:7901850, ECO:0000269|PubMed:8218160, ECO:0000269|PubMed:8262987, ECO:0000269|PubMed:8331673, ECO:0000269|PubMed:8399159, ECO:0000269|PubMed:8431430, ECO:0000269|PubMed:8451242, ECO:0000269|PubMed:8482389, ECO:0000269|PubMed:8639494, ECO:0000269|PubMed:8987974, ECO:0000269|PubMed:9398308, ECO:0000269|PubMed:9865942
|
| source |
Swiss-Prot : SWS_FT_FI3
|
|
|
19)
|
chain |
A |
| residue |
63 |
| type |
SITE |
| sequence |
G
|
| description |
Fine-tunes the proton-transfer properties of H-64; involved in the binding of some activators, including histamine and L-histidine => ECO:0000269|PubMed:16214338, ECO:0000269|PubMed:9265618, ECO:0000305|PubMed:17330962
|
| source |
Swiss-Prot : SWS_FT_FI6
|
|
|
20)
|
chain |
A |
| residue |
68 |
| type |
SITE |
| sequence |
V
|
| description |
Fine-tunes the proton-transfer properties of H-64; involved in the binding of some activators, including histamine and L-histidine => ECO:0000269|PubMed:16214338, ECO:0000269|PubMed:9265618, ECO:0000305|PubMed:17330962
|
| source |
Swiss-Prot : SWS_FT_FI6
|
|
|
|