4QJX

Crystal structure of human carbonic anhydrase isozyme XIII with inhibitor

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	0008270	molecular_function	zinc ion 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	4
Details	BINDING SITE FOR RESIDUE ZN A 301

Chain	Residue
A	HIS96
A	HIS98
A	HIS121
A	WWO304

---

site_id	AC2
Number of Residues	4
Details	BINDING SITE FOR RESIDUE PEG A 302

Chain	Residue
A	SER190
A	GLN216
A	HOH503
A	HOH598

---

site_id	AC3
Number of Residues	5
Details	BINDING SITE FOR RESIDUE EDO A 303

Chain	Residue
A	ARG177
A	PHE178
A	THR179
A	HOH593
A	LYS161

---

site_id	AC4
Number of Residues	13
Details	BINDING SITE FOR RESIDUE WWO A 304

Chain	Residue
A	SER64
A	HIS66
A	ASN69
A	HIS96
A	HIS98
A	HIS121
A	PHE133
A	ALA137
A	LEU200
A	THR201
A	VAL202
A	ZN301
A	HOH546

---

Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
A	SER107-VAL123

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	1
Details	Active site: {"description":"Proton donor/acceptor","evidences":[{"source":"UniProtKB","id":"P00918","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI2
Number of Residues	3
Details	Binding site: {"evidences":[{"source":"PubMed","id":"18618712","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI3
Number of Residues	1
Details	Binding site: {"evidences":[{"source":"UniProtKB","id":"P00918","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

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