eF-site ID 5l9e-B
PDB Code 5l9e
Chain B

click to enlarge
Title CRYSTAL STRUCTURE OF HUMAN CARBONIC ANHYDRASE II IN COMPLEX WITH A QUINOLINE OLIGOAMIDE FOLDAMER
Classification Lyase/Inhibitor
Compound Carbonic anhydrase 2
Source (5L9E)
Sequence B:  SHHWGYGKHNGPEHWHKDFPIAKGERQSPVDIDTHTAKYD
PSLKPLSVSYDQATSLRILNNGHAFNVEFDDSQDKAVLKG
GPLDGTYRLIQFHFHWGSLDGQGSEHTVDKKKYAAELHLV
HWNTKYGDFGKAVQQPDGLAVLGIFLKVGSAKPGLQKVVD
VLDSIKTKGKSADFTNFDPRGLLPESLDYWTYPGSLTTPP
LLECVTWIVLKEPISVSSEQVLKFRKLNFNGEGEPEELMV
DNWRPAQPLKNRQIKASFK
Description


Functional site

1) chain B
residue 189
type
sequence D
description binding site for residue ZN A 306
source : AC6

2) chain B
residue 52
type
sequence D
description binding site for residue ZN A 307
source : AC7

3) chain B
residue 186
type
sequence E
description binding site for residue ZN A 310
source : AD1

4) chain B
residue 94
type
sequence H
description binding site for residue ZN B 301
source : AD3

5) chain B
residue 96
type
sequence H
description binding site for residue ZN B 301
source : AD3

6) chain B
residue 119
type
sequence H
description binding site for residue ZN B 301
source : AD3

7) chain B
residue 4
type
sequence H
description binding site for residue ZN B 302
source : AD4

8) chain B
residue 64
type
sequence H
description binding site for residue ZN B 302
source : AD4

9) chain B
residue 17
type
sequence H
description binding site for residue ZN B 303
source : AD5

10) chain B
residue 18
type
sequence K
description binding site for residue ZN B 303
source : AD5

11) chain B
residue 174
type
sequence D
description binding site for residue ZN B 304
source : AD6

12) chain B
residue 34
type
sequence D
description binding site for residue ZN B 305
source : AD7

13) chain B
residue 36
type
sequence H
description binding site for residue ZN B 305
source : AD7

14) chain B
residue 62
type
sequence N
description binding site for residue GOL B 306
source : AD8

15) chain B
residue 65
type
sequence A
description binding site for residue GOL B 306
source : AD8

16) chain B
residue 67
type
sequence N
description binding site for residue GOL B 306
source : AD8

17) chain B
residue 92
type
sequence Q
description binding site for residue GOL B 306
source : AD8

18) chain B
residue 14
type
sequence E
description binding site for residue ZN C 305
source : AE4

19) chain B
residue 10
type
sequence H
description binding site for residue ZN C 307
source : AE6

20) chain B
residue 26
type
sequence E
description binding site for residue ZN D 303
source : AE9

21) chain B
residue 233
type
sequence E
description binding site for residue ZN D 307
source : AF4

22) chain B
residue 233
type
sequence E
description binding site for residue ZN D 307
source : AF4

23) chain B
residue 4
type
sequence H
description binding site for residues QUJ B 303 and QVE B 304
source : AG1

24) chain B
residue 4
type
sequence H
description binding site for residues QVE B 304 and QUJ B 305
source : AG2

25) chain B
residue 19
type
sequence D
description binding site for residues QVE B 304 and QUJ B 305
source : AG2

26) chain B
residue 20
type
sequence F
description binding site for residues QVE B 304 and QUJ B 305
source : AG2

27) chain B
residue 4
type
sequence H
description binding site for residues QUJ B 305 and QVE B 306
source : AG3

28) chain B
residue 5
type
sequence W
description binding site for residues QUJ B 305 and QVE B 306
source : AG3

29) chain B
residue 19
type
sequence D
description binding site for residues QUJ B 305 and QVE B 306
source : AG3

30) chain B
residue 20
type
sequence F
description binding site for residues QUJ B 305 and QVE B 306
source : AG3

31) chain B
residue 64
type
sequence H
description binding site for residues QUJ B 305 and QVE B 306
source : AG3

32) chain B
residue 201
type
sequence P
description binding site for residues QUJ B 305 and QVE B 306
source : AG3

33) chain B
residue 4
type
sequence H
description binding site for residues QUJ B 312 and QVE D 304
source : AG4

34) chain B
residue 19
type
sequence D
description binding site for residues QUJ B 312 and QVE D 305
source : AG5

35) chain B
residue 20
type
sequence F
description binding site for residues QUJ B 312 and QVE D 305
source : AG5

36) chain B
residue 64
type catalytic
sequence H
description 216
source MCSA : MCSA2

37) chain B
residue 94
type catalytic
sequence H
description 216
source MCSA : MCSA2

38) chain B
residue 96
type catalytic
sequence H
description 216
source MCSA : MCSA2

39) chain B
residue 106
type catalytic
sequence E
description 216
source MCSA : MCSA2

40) chain B
residue 119
type catalytic
sequence H
description 216
source MCSA : MCSA2

41) chain B
residue 198
type catalytic
sequence T
description 216
source MCSA : MCSA2

42) 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

43) 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

44) 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

45) 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

46) chain B
residue 198
type BINDING
sequence T
description BINDING => ECO:0000269|PubMed:10550681, ECO:0000269|PubMed:19520834
source Swiss-Prot : SWS_FT_FI4

47) 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

48) 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

49) chain B
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

50) 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

51) chain B
residue 2
type MOD_RES
sequence S
description Phosphoserine => ECO:0000250|UniProtKB:P27139
source Swiss-Prot : SWS_FT_FI8

52) chain B
residue 165
type MOD_RES
sequence S
description Phosphoserine => ECO:0007744|PubMed:24275569
source Swiss-Prot : SWS_FT_FI9

53) chain B
residue 172
type MOD_RES
sequence S
description Phosphoserine => ECO:0007744|PubMed:24275569
source Swiss-Prot : SWS_FT_FI9


Display surface

Download
Links