eF-site ID 6oe0-A
PDB Code 6oe0
Chain A

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Title Benzensulfonamides bearing spyrohydantoin moieties act as potent inhibitors of human carbonic anhydrases II and VII and show neuropathic pain attenuating effects
Classification LYASE/LYASE INHIBITOR
Compound Carbonic anhydrase 2
Source (CAH2_HUMAN)
Sequence A:  HHWGYGKHNGPEHWHKDFPIAKGERQSPVDIDTHTAKYDP
SLKPLSVSYDQATSLRILNNGHAFNVEFDDSQDKAVLKGG
PLDGTYRLIQFHFHWGSLDGQGSEHTVDKKKYAAELHLVH
WNTKYGDFGKAVQQPDGLAVLGIFLKVGSAKPGLQKVVDV
LDSIKTKGKSADFTNFDPRGLLPESLDYWTYPGSLTTPPL
LECVTWIVLKEPISVSSEQVLKFRKLNFNGEGEPEELMVD
NWRPAQPLKNRQIKASFK
Description


Functional site

1) chain A
residue 94
type
sequence H
description binding site for residue ZN A 301
source : AC1

2) chain A
residue 96
type
sequence H
description binding site for residue ZN A 301
source : AC1

3) chain A
residue 119
type
sequence H
description binding site for residue ZN A 301
source : AC1

4) chain A
residue 67
type
sequence N
description binding site for residue M8S A 302
source : AC2

5) chain A
residue 91
type
sequence I
description binding site for residue M8S A 302
source : AC2

6) chain A
residue 92
type
sequence Q
description binding site for residue M8S A 302
source : AC2

7) chain A
residue 94
type
sequence H
description binding site for residue M8S A 302
source : AC2

8) chain A
residue 96
type
sequence H
description binding site for residue M8S A 302
source : AC2

9) chain A
residue 119
type
sequence H
description binding site for residue M8S A 302
source : AC2

10) chain A
residue 131
type
sequence F
description binding site for residue M8S A 302
source : AC2

11) chain A
residue 198
type
sequence L
description binding site for residue M8S A 302
source : AC2

12) chain A
residue 199
type
sequence T
description binding site for residue M8S A 302
source : AC2

13) chain A
residue 200
type
sequence T
description binding site for residue M8S A 302
source : AC2

14) chain A
residue 209
type
sequence W
description binding site for residue M8S A 302
source : AC2

15) chain A
residue 62
type
sequence N
description binding site for residue GOL A 303
source : AC3

16) chain A
residue 64
type
sequence H
description binding site for residue GOL A 303
source : AC3

17) chain A
residue 65
type
sequence A
description binding site for residue GOL A 303
source : AC3

18) chain A
residue 67
type
sequence N
description binding site for residue GOL A 303
source : AC3

19) chain A
residue 92
type
sequence Q
description binding site for residue GOL A 303
source : AC3

20) chain A
residue 94
type
sequence H
description binding site for residue GOL A 303
source : AC3

21) chain A
residue 200
type
sequence T
description binding site for residue GOL A 303
source : AC3

22) chain A
residue 64
type catalytic
sequence H
description 216
source MCSA : MCSA1

23) chain A
residue 94
type catalytic
sequence H
description 216
source MCSA : MCSA1

24) chain A
residue 96
type catalytic
sequence H
description 216
source MCSA : MCSA1

25) chain A
residue 106
type catalytic
sequence E
description 216
source MCSA : MCSA1

26) chain A
residue 119
type catalytic
sequence H
description 216
source MCSA : MCSA1

27) chain A
residue 199
type catalytic
sequence T
description 216
source MCSA : MCSA1

28) chain A
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

29) chain A
residue 199
type BINDING
sequence T
description BINDING => ECO:0000269|PubMed:10550681, ECO:0000269|PubMed:19520834
source Swiss-Prot : SWS_FT_FI4

30) 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

31) 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

32) 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

33) chain A
residue 105-121
type prosite
sequence SEHTVDKKKYAAELHLV
description ALPHA_CA_1 Alpha-carbonic anhydrases signature. SEHtVdkkkYaaELHLV
source prosite : PS00162

34) 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

35) 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
source Swiss-Prot : SWS_FT_FI3

36) 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
source Swiss-Prot : SWS_FT_FI3

37) 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
source Swiss-Prot : SWS_FT_FI7

38) chain A
residue 166
type MOD_RES
sequence S
description Phosphoserine => ECO:0007744|PubMed:24275569
source Swiss-Prot : SWS_FT_FI9

39) chain A
residue 173
type MOD_RES
sequence S
description Phosphoserine => ECO:0007744|PubMed:24275569
source Swiss-Prot : SWS_FT_FI9


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