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eF-site ID
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6gm9-A |
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PDB Code
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6gm9 |
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Chain
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A |
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click to enlarge
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Title
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Human Carbonic Anhydrase II in complex with 4-Methylbenzenesulfonamide |
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Classification
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LYASE |
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Compound
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Carbonic anhydrase 2 |
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Source
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(CAH2_HUMAN) |
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Sequence
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A: |
HWGYGKHNGPEHWHKDFPIAKGERQSPVDIDTHTAKYDPS
LKPLSVSYDQATSLRILNNGHAFNVEFDDSQDKAVLKGGP
LDGTYRLIQFHFHWGSLDGQGSEHTVDKKKYAAELHLVHW
NTKYGDFGKAVQQPDGLAVLGIFLKVGSAKPGLQKVVDVL
DSIKTKGKSADFTNFDPRGLLPESLDYWTYPGSLTTPPLL
ECVTWIVLKEPISVSSEQVLKFRKLNFNGEGEPEELMVDN
WRPAQPLKNRQIKASFK
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Description
|
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Functional site
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|
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1)
|
chain |
A |
| residue |
92 |
| type |
SITE |
| sequence |
Q
|
| 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
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| source |
Swiss-Prot : SWS_FT_FI7
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|
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2)
|
chain |
A |
| residue |
166 |
| type |
MOD_RES |
| sequence |
S
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| description |
Phosphoserine => ECO:0007744|PubMed:24275569
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| source |
Swiss-Prot : SWS_FT_FI9
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|
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3)
|
chain |
A |
| residue |
173 |
| type |
MOD_RES |
| sequence |
S
|
| description |
Phosphoserine => ECO:0007744|PubMed:24275569
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| source |
Swiss-Prot : SWS_FT_FI9
|
|
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4)
|
chain |
A |
| residue |
119 |
| type |
BINDING |
| sequence |
H
|
| 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
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| source |
Swiss-Prot : SWS_FT_FI3
|
|
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5)
|
chain |
A |
| residue |
96 |
| type |
BINDING |
| sequence |
H
|
| 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
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| source |
Swiss-Prot : SWS_FT_FI3
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|
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6)
|
chain |
A |
| residue |
67 |
| type |
SITE |
| sequence |
N
|
| 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
|
|
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7)
|
chain |
A |
| residue |
62 |
| type |
SITE |
| sequence |
N
|
| 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
|
|
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8)
|
chain |
A |
| residue |
105-121 |
| type |
prosite |
| sequence |
SEHTVDKKKYAAELHLV
|
| description |
ALPHA_CA_1 Alpha-carbonic anhydrases signature. SEHtVdkkkYaaELHLV
|
| source |
prosite : PS00162
|
|
|
9)
|
chain |
A |
| residue |
64 |
| type |
catalytic |
| sequence |
H
|
| description |
216
|
| source |
MCSA : MCSA1
|
|
|
10)
|
chain |
A |
| residue |
94 |
| type |
catalytic |
| sequence |
H
|
| description |
216
|
| source |
MCSA : MCSA1
|
|
|
11)
|
chain |
A |
| residue |
96 |
| type |
catalytic |
| sequence |
H
|
| description |
216
|
| source |
MCSA : MCSA1
|
|
|
12)
|
chain |
A |
| residue |
106 |
| type |
catalytic |
| sequence |
E
|
| description |
216
|
| source |
MCSA : MCSA1
|
|
|
13)
|
chain |
A |
| residue |
119 |
| type |
catalytic |
| sequence |
H
|
| description |
216
|
| source |
MCSA : MCSA1
|
|
|
14)
|
chain |
A |
| residue |
199 |
| type |
catalytic |
| sequence |
T
|
| description |
216
|
| source |
MCSA : MCSA1
|
|
|
15)
|
chain |
A |
| residue |
64 |
| type |
ACT_SITE |
| sequence |
H
|
| description |
Proton donor/acceptor => ECO:0000305|PubMed:15667203, ECO:0000305|PubMed:17330962
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| source |
Swiss-Prot : SWS_FT_FI1
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|
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16)
|
chain |
A |
| residue |
94 |
| type |
BINDING |
| sequence |
H
|
| 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
|
|
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17)
|
chain |
A |
| residue |
199 |
| type |
BINDING |
| sequence |
T
|
| description |
BINDING => ECO:0000269|PubMed:10550681, ECO:0000269|PubMed:19520834
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| source |
Swiss-Prot : SWS_FT_FI4
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|
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18)
|
chain |
A |
| residue |
7 |
| type |
SITE |
| sequence |
Y
|
| description |
Fine-tunes the proton-transfer properties of H-64 => ECO:0000305|PubMed:17330962
|
| source |
Swiss-Prot : SWS_FT_FI5
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