5MSB

Crystal structure of human carbonic anhydrase isozyme XII with 2,3,5,6-tetrafluoro-4[(2-hydroxyethyl)sulfonyl]benzenesulfonamide

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 PDB Data

site_id	AC1
Number of Residues	4
Details	binding site for residue ZN A 301

Chain	Residue
A	HIS91
A	HIS93
A	HIS117
A	V13303

---

site_id	AC2
Number of Residues	5
Details	binding site for residue EDO A 302

Chain	Residue
A	GLU147
A	PRO214
A	GLN216
A	HOH416
A	HOH458

---

site_id	AC3
Number of Residues	15
Details	binding site for residue V13 A 303

Chain	Residue
A	GLN89
A	HIS91
A	HIS93
A	HIS117
A	VAL119
A	LEU139
A	VAL141
A	LEU197
A	THR198
A	THR199
A	TRP208
A	ZN301
A	HOH552
A	HOH580
A	HOH625

---

site_id	AC4
Number of Residues	4
Details	binding site for residue ZN B 301

Chain	Residue
B	HIS91
B	HIS93
B	HIS117
B	V13305

---

site_id	AC5
Number of Residues	7
Details	binding site for residue PEG B 302

Chain	Residue
B	VAL107
B	GLN110
B	HIS111
B	PHE112
B	HOH409
B	HOH529
B	HOH581

---

site_id	AC6
Number of Residues	7
Details	binding site for residue EDO B 303

Chain	Residue
A	PHE7
A	ASN244
A	HOH572
B	LYS251
B	ASP253
B	HOH406
B	HOH487

---

site_id	AC7
Number of Residues	2
Details	binding site for residue EDO B 304

Chain	Residue
B	ARG212
B	ASN213

---

site_id	AC8
Number of Residues	18
Details	binding site for residue V13 B 305

Chain	Residue
B	GLN89
B	HIS91
B	HIS93
B	HIS117
B	VAL119
B	ALA129
B	LEU139
B	VAL141
B	LEU197
B	THR198
B	THR199
B	PRO200
B	PRO201
B	TRP208
B	ZN301
B	HOH407
B	HOH503
B	HOH606

---

site_id	AC9
Number of Residues	4
Details	binding site for residue ZN C 301

Chain	Residue
C	HIS91
C	HIS93
C	HIS117
C	V13302

---

site_id	AD1
Number of Residues	14
Details	binding site for residue V13 C 302

Chain	Residue
C	GLN89
C	HIS91
C	HIS93
C	HIS117
C	VAL119
C	LEU139
C	VAL141
C	LEU197
C	THR198
C	THR199
C	TRP208
C	ZN301
C	HOH560
C	HOH567

---

site_id	AD2
Number of Residues	4
Details	binding site for residue ZN D 301

Chain	Residue
D	HIS91
D	HIS93
D	HIS117
D	V13305

---

site_id	AD3
Number of Residues	6
Details	binding site for residue EDO D 302

Chain	Residue
D	SER42
D	THR44
D	GLY80
D	TYR190
D	ARG192
D	HOH569

---

site_id	AD4
Number of Residues	3
Details	binding site for residue EDO D 303

Chain	Residue
D	LEU43
D	ARG192
D	HOH569

---

site_id	AD5
Number of Residues	7
Details	binding site for residue EDO D 304

Chain	Residue
D	HOH527
D	SER133
D	ASN134
D	PRO201
D	ASN203
D	HOH430
D	HOH452

---

site_id	AD6
Number of Residues	16
Details	binding site for residue V13 D 305

Chain	Residue
D	GLN89
D	HIS91
D	HIS93
D	HIS117
D	VAL119
D	ALA129
D	SER130
D	LEU139
D	VAL141
D	LEU197
D	THR198
D	THR199
D	TRP208
D	ZN301
D	HOH422
D	HOH577

---

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	SER103-VAL119

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	4
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	12
Details	Binding site: {"evidences":[{"source":"PubMed","id":"11493685","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI3
Number of Residues	4
Details	Binding site: {"evidences":[{"source":"UniProtKB","id":"P00918","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI4
Number of Residues	8
Details	Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---