eF-site ID 1cvd-A
PDB Code 1cvd
Chain A

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Title STRUCTURAL CONSEQUENCES OF REDESIGNING A PROTEIN-ZINC BINDING SITE
Classification LYASE(OXO-ACID)
Compound CARBONIC ANHYDRASE II
Source Homo sapiens (Human) (CAH2_HUMAN)
Sequence A:  WGYGKHNGPEHWHKDFPIAKGERQSPVDIDTHTAKYDPSL
KPLSVSYDQATSLRILNNGHAFNVEFDDSQDKAVLKGGPL
DGTYRLIQFHFHWGSLDGQGSEHTVDKKKYAAELCLVHWN
TKYGDFGKAVQQPDGLAVLGIFLKVGSAKPGLQKVVDVLD
SIKTKGKSADFTNFDPRGLLPESLDYWTYPGSLTTPPLLE
CVTWIVLKEPISVSSEQVLKFRKLNFNGEGEPEELMVDNW
RPAQPLKNRQIKASF
Description (1)  CARBONIC ANHYDRASE II (CARBONATE DEHYDRATASE) (HCA II) (E.C.4.2.1.1) MUTANT WITH HIS 119 REPLACED BY CYS (H119C)


Functional site

1) chain A
residue 94
type
ligand
sequence H
description BINDING SITE FOR RESIDUE ZN A 262
source : AC1

2) chain A
residue 96
type
ligand
sequence H
description BINDING SITE FOR RESIDUE ZN A 262
source : AC1

3) chain A
residue 119
type
ligand
sequence C
description BINDING SITE FOR RESIDUE ZN A 262
source : AC1

4) chain A
residue 63
type ACT_SITE
ligand
sequence G
description {ECO:0000269|PubMed:15667203, ECO:0000269|PubMed:17330962, ECO:0000269|PubMed:19170619}.
source Swiss-Prot : SWS_FT_FI1

5) chain A
residue 123
type ACT_SITE
ligand
sequence W
description {ECO:0000269|PubMed:15667203, ECO:0000269|PubMed:17330962, ECO:0000269|PubMed:19170619}.
source Swiss-Prot : SWS_FT_FI1

6) chain A
residue 60
type ACT_SITE
ligand
sequence L
description Proton acceptor. {ECO:0000269|PubMed:15667203, ECO:0000269|PubMed:17330962, ECO:0000269|PubMed:19170619}.
source Swiss-Prot : SWS_FT_FI2

7) chain A
residue 92
type METAL
ligand
sequence Q
description Zinc; catalytic. {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

8) chain A
residue 115
type METAL
ligand
sequence A
description Zinc; catalytic. {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

9) chain A
residue 90
type METAL
ligand
sequence L
description Zinc; catalytic. {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_FI4

10) chain A
residue 58
type BINDING
ligand
sequence R
description Activator. {ECO:0000269|PubMed:16214338, ECO:0000269|PubMed:17127057, ECO:0000269|PubMed:9265618}.
source Swiss-Prot : SWS_FT_FI5

11) chain A
residue 63
type BINDING
ligand
sequence G
description Activator. {ECO:0000269|PubMed:16214338, ECO:0000269|PubMed:17127057, ECO:0000269|PubMed:9265618}.
source Swiss-Prot : SWS_FT_FI5

12) chain A
residue 88
type BINDING
ligand
sequence Y
description Activator. {ECO:0000269|PubMed:16214338, ECO:0000269|PubMed:17127057, ECO:0000269|PubMed:9265618}.
source Swiss-Prot : SWS_FT_FI5

13) chain A
residue 199
type catalytic
ligand
sequence T
description Annotated By Reference To The Literature 1ca2
source CSA : CSA1

14) chain A
residue 64
type catalytic
ligand
sequence H
description Annotated By Reference To The Literature 1ca2
source CSA : CSA1


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