8Q1A

The Crystal Structure of Human Carbonic Anhydrase IX in Complex with inhibitor

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. SEHtVeghrFpaEIHVV

Chain	Residue	Details
A	SER105-VAL121

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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	HIS68
B	HIS68
C	HIS68
D	HIS68

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site_id	SWS_FT_FI2
Number of Residues	12
Details	BINDING: BINDING => ECO:0000269|PubMed:19805286

Chain	Residue	Details
A	HIS94
D	HIS94
D	HIS96
D	HIS119
A	HIS96
A	HIS119
B	HIS94
B	HIS96
B	HIS119
C	HIS94
C	HIS96
C	HIS119

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

Chain	Residue	Details
A	THR200
B	THR200
C	THR200
D	THR200

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site_id	SWS_FT_FI4
Number of Residues	4
Details	CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:18703501, ECO:0000269|PubMed:19805286

Chain	Residue	Details
A	GLN214
B	GLN214
C	GLN214
D	GLN214

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