8CO3

Three dimensional structure of human carbonic anhydrase XII in complex with sulfonamide

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004089	molecular_function	carbonate dehydratase activity
A	0008270	molecular_function	zinc ion binding
B	0004089	molecular_function	carbonate dehydratase activity
B	0008270	molecular_function	zinc ion binding
C	0004089	molecular_function	carbonate dehydratase activity
C	0008270	molecular_function	zinc ion binding
D	0004089	molecular_function	carbonate dehydratase activity
D	0008270	molecular_function	zinc ion binding

Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
A	SER109-VAL125

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	4
Details	ACT_SITE: Proton donor/acceptor => ECO:0000250|UniProtKB:P00918

Chain	Residue	Details
A	HIS67
B	HIS67
C	HIS67
D	HIS67

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site_id	SWS_FT_FI2
Number of Residues	12
Details	BINDING: BINDING => ECO:0000269|PubMed:11493685

Chain	Residue	Details
A	HIS97
A	HIS99
A	HIS123
B	HIS97
B	HIS99
B	HIS123
C	HIS97
C	HIS99
C	HIS123
D	HIS97
D	HIS99
D	HIS123

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site_id	SWS_FT_FI3
Number of Residues	4
Details	BINDING: BINDING => ECO:0000250|UniProtKB:P00918

Chain	Residue	Details
A	THR204
B	THR204
C	THR204
D	THR204

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site_id	SWS_FT_FI4
Number of Residues	8
Details	CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255

Chain	Residue	Details
A	ASN53
A	ASN140
B	ASN53
B	ASN140
C	ASN53
C	ASN140
D	ASN53
D	ASN140

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