1KOQ

NEISSERIA GONORRHOEAE CARBONIC ANHYDRASE

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004089	molecular_function	carbonate dehydratase activity
A	0006885	biological_process	regulation of pH
A	0008270	molecular_function	zinc ion binding
A	0015670	biological_process	carbon dioxide transport
A	0016829	molecular_function	lyase activity
A	0042597	cellular_component	periplasmic space
A	0046872	molecular_function	metal ion binding
B	0004089	molecular_function	carbonate dehydratase activity
B	0006885	biological_process	regulation of pH
B	0008270	molecular_function	zinc ion binding
B	0015670	biological_process	carbon dioxide transport
B	0016829	molecular_function	lyase activity
B	0042597	cellular_component	periplasmic space
B	0046872	molecular_function	metal ion binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN A 301

Chain	Residue
A	HIS92
A	HIS94
A	HIS111
A	HOH303

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site_id	AC2
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN B 302

Chain	Residue
B	HIS92
B	HIS94
B	HIS111
B	HOH305

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Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
A	SER97-VAL113

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	2
Details	ACT_SITE: Proton acceptor => ECO:0000250|UniProtKB:P00918

Chain	Residue	Details
A	HIS66
B	HIS66

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site_id	SWS_FT_FI2
Number of Residues	8
Details	BINDING: BINDING => ECO:0000269|PubMed:9761692

Chain	Residue	Details
A	HIS92
A	HIS94
A	HIS111
A	THR177
B	HIS92
B	HIS94
B	HIS111
B	THR177

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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	THR177
A	HIS66

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site_id	CSA2
Number of Residues	2
Details	Annotated By Reference To The Literature 1ca2

Chain	Residue	Details
B	THR177
B	HIS66

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