Structure of PDB 5e2n Chain A

Receptor sequence
>5e2nA (length=258) Species: 9606 (Homo sapiens) [Search protein sequence]
SWGYREHNGPIHWKEFFPIADGDQQSPIEIKTKEVKYDSSLRPLSIKYDP
SSAKIISNSGHSFNVDFDDTENKSVLRGGPLTGSYRLRQVHLHWGSADDH
GSEHIVDGVSYAAELHVVHWNSDKYPSFVEAAHEPDGLAVLGVFLQIGEP
NSQLQKITDTLDSIKEKGKQTRFTNFDLLSLLPPSWDYWTYPGSLTVPPL
LESVTWIVLKQPINISSQQLAKFRSLLCTAEGEAAAFLVSNHRPPQPLKG
RKVRASFH
3D structure
PDB5e2n Intrinsic Thermodynamics and Structures of 2,4- and 3,4-Substituted Fluorinated Benzenesulfonamides Binding to Carbonic Anhydrases.
ChainA
Resolution1.53 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) H66 H96 H98 E108 H121 T201
Catalytic site (residue number reindexed from 1) H61 H91 H93 E103 H116 T196
Enzyme Commision number 4.2.1.1: carbonic anhydrase.
Interaction with ligand
Site
#		 Ligand Ligand
chain		 Binding residues on receptor
(original residue number in PDB)		 Binding residues on receptor
(residue number reindexed from 1)		 Binding affinity
BS01 ZN A H96 H98 H121 H91 H93 H116
BS02 V14 A W7 S64 H66 S67 N69 Q94 H96 H98 V123 F133 L200 T201 V202 W2 S59 H61 S62 N64 Q89 H91 H93 V118 F128 L195 T196 V197 MOAD: Kd=0.29nM
PDBbind-CN: -logKd/Ki=9.54,Kd=0.29nM
BindingDB: Kd=42nM
Gene Ontology
Molecular Function
GO:0004089 carbonate dehydratase activity
GO:0005515 protein binding
GO:0008270 zinc ion binding
GO:0016829 lyase activity
GO:0046872 metal ion binding
Biological Process
GO:0006730 one-carbon metabolic process
Cellular Component
GO:0005737 cytoplasm
GO:0005829 cytosol
GO:0043209 myelin sheath
GO:0043231 intracellular membrane-bounded organelle

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Molecular Function
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Cellular Component
External links
PDB RCSB:5e2n, PDBe:5e2n, PDBj:5e2n
PDBsum5e2n
PubMed28001003
UniProtQ8N1Q1|CAH13_HUMAN Carbonic anhydrase 13 (Gene Name=CA13)

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