Structure of PDB 6h38 Chain A

Receptor sequence
>6h38A (length=259) Species: 9606 (Homo sapiens) [Search protein sequence]
GWGYGQDDGPSHWHKLYPIAQGDRQSPINIISSQAVYSPSLQPLELSYEA
CMSLSITNNGHSVQVDFNDSDDRTVVTGGPLEGPYRLKQFHFHWGKKHDV
GSEHTVDGKSFPSELHLVHWNAKKYSTFGEAASAPDGLAVVGVFLETGDE
HPSMNRLTDALYMVRFKGTKAQFSCFNPKSLLPASRHYWTYPGSLTTPPL
SESVTWIVLREPISISERQMGKFRSLLFTSEDDERIHMVNNFRPPQPLKG
RVVKASFRA
3D structure
PDB6h38 Exploring structural properties of potent human carbonic anhydrase inhibitors bearing a 4-(cycloalkylamino-1-carbonyl)benzenesulfonamide moiety.
ChainA
Resolution1.7 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) H64 H94 H96 E106 H119 T199
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 H94 H96 H119 H91 H93 H116
BS02 FKK A Y20 Q92 H94 H119 V121 F131 L198 T199 T200 P201 P202 Y17 Q89 H91 H116 V118 F128 L195 T196 T197 P198 P199 MOAD: Ki=7.8nM
PDBbind-CN: -logKd/Ki=8.11,Ki=7.8nM
BindingDB: Ki=7.8nM
Gene Ontology
Molecular Function
GO:0004089 carbonate dehydratase activity
GO:0008270 zinc ion binding
GO:0016829 lyase activity
GO:0046872 metal ion binding
Biological Process
GO:0006730 one-carbon metabolic process
GO:0032230 positive regulation of synaptic transmission, GABAergic
GO:0032849 positive regulation of cellular pH reduction
GO:0051453 regulation of intracellular pH
GO:0070050 neuron cellular homeostasis
GO:2001225 regulation of chloride transport
Cellular Component
GO:0005737 cytoplasm
GO:0005829 cytosol

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Cellular Component
External links
PDB RCSB:6h38, PDBe:6h38, PDBj:6h38
PDBsum6h38
PubMed30530195
UniProtP43166|CAH7_HUMAN Carbonic anhydrase 7 (Gene Name=CA7)

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