5LLP

Crystal structure of human carbonic anhydrase isozyme XII with 3-[(1S)-1,2,3,4-Tetrahydronapthalen-1-ylamino)-2,5,6-trifluoro-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	6Z9302

---

site_id	AC2
Number of Residues	16
Details	binding site for residue 6Z9 A 302

Chain	Residue
A	HIS93
A	GLU104
A	HIS117
A	ALA129
A	SER133
A	LEU197
A	THR198
A	THR199
A	PRO200
A	ZN301
A	HOH623
A	TRP4
A	ASN64
A	LYS69
A	GLN89
A	HIS91

---

site_id	AC3
Number of Residues	4
Details	binding site for residue ZN B 301

Chain	Residue
B	HIS91
B	HIS93
B	HIS117
B	6Z9302

---

site_id	AC4
Number of Residues	12
Details	binding site for residue 6Z9 B 302

Chain	Residue
B	ASN64
B	SER67
B	HIS91
B	HIS93
B	HIS117
B	ALA129
B	LEU197
B	THR198
B	THR199
B	PRO200
B	ZN301
B	HOH439

---

site_id	AC5
Number of Residues	4
Details	binding site for residue ZN C 301

Chain	Residue
C	HIS91
C	HIS93
C	HIS117
C	6Z9302

---

site_id	AC6
Number of Residues	13
Details	binding site for residue 6Z9 C 302

Chain	Residue
C	ASN64
C	LYS69
C	GLN89
C	HIS91
C	HIS93
C	GLU104
C	HIS117
C	ALA129
C	LEU197
C	THR198
C	THR199
C	PRO201
C	ZN301

---

site_id	AC7
Number of Residues	4
Details	binding site for residue ZN D 301

Chain	Residue
D	HIS91
D	HIS93
D	HIS117
D	6Z9302

---

site_id	AC8
Number of Residues	14
Details	binding site for residue 6Z9 D 302

Chain	Residue
D	ASN64
D	HIS91
D	HIS93
D	HIS117
D	VAL119
D	ALA129
D	SER130
D	LEU197
D	THR198
D	THR199
D	PRO200
D	ZN301
D	HOH406
D	HOH513

---

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	ACT_SITE: Proton donor/acceptor => ECO:0000250|UniProtKB:P00918

Chain	Residue	Details
A	HIS66
B	HIS66
C	HIS66
D	HIS66

---

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

Chain	Residue	Details
A	HIS91
D	HIS91
D	HIS93
D	HIS117
A	HIS93
A	HIS117
B	HIS91
B	HIS93
B	HIS117
C	HIS91
C	HIS93
C	HIS117

---

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

Chain	Residue	Details
A	THR198
B	THR198
C	THR198
D	THR198

---

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

Chain	Residue	Details
A	ASN52
A	ASN134
B	ASN52
B	ASN134
C	ASN52
C	ASN134
D	ASN52
D	ASN134

---