eF-site ID 5ogn-B
PDB Code 5ogn
Chain B

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Title Metalacarborane inhibitors of Carbonic Anhydrase IX
Classification LYASE
Compound Carbonic anhydrase 2
Source (CAH2_HUMAN)
Sequence B:  HHWGYGKHNGPEHWHKDFPIAKGERQSPVDIDTHTAKYDP
SLKPLSVSYDQATSLRILNNGHSFQVTFDDSQDKAVLKGG
PLDGTYRLLQFHFHWGSLDGQGSEHTVDKKKYAAELHLVH
WNTKYGDVGKAVQQPDGLAVLGIFLKVGSAKPGLQKVVDV
LDSIKTEGKSADFTNFDPRGLLPESLDYWTYPGSLTTPPL
AECVTWIVLKEPISVSSEQVLKFRKLNFNGEGEPEELMVD
NWRPAQPLKNRQIKASFK
Description


Functional site
1) chain B
residue 4
type
sequence H
description binding site for residue ZN A 303
source : AC3
2) chain B
residue 64
type
sequence H
description binding site for residue ZN A 303
source : AC3
3) chain B
residue 94
type
sequence H
description binding site for residue ZN B 301
source : AC4
4) chain B
residue 96
type
sequence H
description binding site for residue ZN B 301
source : AC4
5) chain B
residue 119
type
sequence H
description binding site for residue ZN B 301
source : AC4
6) chain B
residue 92
type
sequence Q
description binding site for residue B8B B 302
source : AC5
7) chain B
residue 94
type
sequence H
description binding site for residue B8B B 302
source : AC5
8) chain B
residue 96
type
sequence H
description binding site for residue B8B B 302
source : AC5
9) chain B
residue 119
type
sequence H
description binding site for residue B8B B 302
source : AC5
10) chain B
residue 197
type
sequence L
description binding site for residue B8B B 302
source : AC5
11) chain B
residue 198
type
sequence T
description binding site for residue B8B B 302
source : AC5
12) chain B
residue 199
type
sequence T
description binding site for residue B8B B 302
source : AC5
13) chain B
residue 200
type
sequence P
description binding site for residue B8B B 302
source : AC5
14) chain B
residue 64
type catalytic
sequence H
description 216
source MCSA : MCSA2
15) chain B
residue 94
type catalytic
sequence H
description 216
source MCSA : MCSA2
16) chain B
residue 96
type catalytic
sequence H
description 216
source MCSA : MCSA2
17) chain B
residue 106
type catalytic
sequence E
description 216
source MCSA : MCSA2
18) chain B
residue 119
type catalytic
sequence H
description 216
source MCSA : MCSA2
19) chain B
residue 198
type catalytic
sequence T
description 216
source MCSA : MCSA2
20) chain B
residue 64
type ACT_SITE
sequence H
description Proton donor/acceptor => ECO:0000305|PubMed:15667203, ECO:0000305|PubMed:17330962
source Swiss-Prot : SWS_FT_FI1
21) chain B
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
22) chain B
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
source Swiss-Prot : SWS_FT_FI3
23) chain B
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
source Swiss-Prot : SWS_FT_FI3
24) chain B
residue 198
type BINDING
sequence T
description BINDING => ECO:0000269|PubMed:10550681, ECO:0000269|PubMed:19520834
source Swiss-Prot : SWS_FT_FI4
25) chain B
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
26) chain B
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
27) chain B
residue 67
type SITE
sequence Q
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
28) chain B
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
source Swiss-Prot : SWS_FT_FI7
29) chain B
residue 165
type MOD_RES
sequence S
description Phosphoserine => ECO:0007744|PubMed:24275569
source Swiss-Prot : SWS_FT_FI8
30) chain B
residue 172
type MOD_RES
sequence S
description Phosphoserine => ECO:0007744|PubMed:24275569
source Swiss-Prot : SWS_FT_FI8

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