1Z93

Human Carbonic Anhydrase III:Structural and Kinetic study of Catalysis and Proton Transfer.

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004089	molecular_function	carbonate dehydratase activity
A	0005515	molecular_function	protein binding
A	0005737	cellular_component	cytoplasm
A	0005829	cellular_component	cytosol
A	0006730	biological_process	one-carbon metabolic process
A	0008270	molecular_function	zinc ion binding
A	0009617	biological_process	response to bacterium
A	0016151	molecular_function	nickel cation binding
A	0016829	molecular_function	lyase activity
A	0046872	molecular_function	metal ion binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	5
Details	BINDING SITE FOR RESIDUE ZN A 268

Chain	Residue
A	HIS94
A	HIS96
A	HIS119
A	THR199
A	HOH269

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Functional Information from PROSITE/UniProt

site_id	PS00162
Number of Residues	17
Details	ALPHA_CA_1 Alpha-carbonic anhydrases signature. SEHtVdgvkYaaELHLV

Chain	Residue	Details
A	SER105-VAL121

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	3
Details	BINDING: BINDING => ECO:0000269|PubMed:16042381, ECO:0000269|PubMed:17427958

Chain	Residue	Details
A	LEU95
A	TRP97
A	LEU120

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site_id	SWS_FT_FI2
Number of Residues	1
Details	BINDING: BINDING => ECO:0000250|UniProtKB:P00918

Chain	Residue	Details
A	THR200

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site_id	SWS_FT_FI3
Number of Residues	1
Details	MOD_RES: N-acetylalanine => ECO:0000250|UniProtKB:P07450

Chain	Residue	Details
A	LYS3

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site_id	SWS_FT_FI4
Number of Residues	6
Details	MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P14141

Chain	Residue	Details
A	PRO30
A	LEU44
A	VAL49
A	TYR51
A	ALA56
A	ASP221

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site_id	SWS_FT_FI5
Number of Residues	3
Details	MOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:P14141

Chain	Residue	Details
A	TYR74
A	PHE131
A	VAL218

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site_id	SWS_FT_FI6
Number of Residues	1
Details	MOD_RES: Phosphotyrosine => ECO:0000250|UniProtKB:P14141

Chain	Residue	Details
A	ASN129

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site_id	SWS_FT_FI7
Number of Residues	1
Details	MOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:P16015

Chain	Residue	Details
A	LYS178

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site_id	SWS_FT_FI8
Number of Residues	2
Details	MOD_RES: S-glutathionyl cysteine => ECO:0000250|UniProtKB:P14141

Chain	Residue	Details
A	LEU184
A	ARG189

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Catalytic Information from CSA

site_id	CSA1
Number of Residues	2
Details	Annotated By Reference To The Literature 1ca2

Chain	Residue	Details
A	THR199
A	LYS64

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