4HT2

Crystal structure of human carbonic anhydrase isozyme XII with the 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 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	V50302

---

site_id	AC2
Number of Residues	20
Details	BINDING SITE FOR RESIDUE V50 A 302

Chain	Residue
A	SER130
A	LEU139
A	VAL141
A	LEU197
A	THR198
A	THR199
A	PRO200
A	ASN203
A	TRP208
A	ZN301
A	PEG303
A	EDO304
A	HOH543
A	HOH592
A	HOH604
A	GLN89
A	HIS91
A	HIS93
A	HIS117
A	VAL119

---

site_id	AC3
Number of Residues	6
Details	BINDING SITE FOR RESIDUE PEG A 303

Chain	Residue
A	ASN64
A	LYS69
A	GLN89
A	THR199
A	V50302
A	EDO304

---

site_id	AC4
Number of Residues	9
Details	BINDING SITE FOR RESIDUE EDO A 304

Chain	Residue
A	ASN64
A	SER67
A	GLN89
A	HIS91
A	HIS93
A	THR199
A	V50302
A	PEG303
A	HOH498

---

site_id	AC5
Number of Residues	6
Details	BINDING SITE FOR RESIDUE EDO A 305

Chain	Residue
A	SER42
A	LEU43
A	THR44
A	GLY80
A	TYR190
A	ARG192

---

site_id	AC6
Number of Residues	3
Details	BINDING SITE FOR RESIDUE EDO A 306

Chain	Residue
A	ASP40
A	TYR258
A	HOH488

---

site_id	AC7
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN B 301

Chain	Residue
B	HIS91
B	HIS93
B	HIS117
B	V50302

---

site_id	AC8
Number of Residues	14
Details	BINDING SITE FOR RESIDUE V50 B 302

Chain	Residue
B	GLN89
B	HIS91
B	HIS93
B	HIS117
B	VAL119
B	SER133
B	LEU197
B	THR198
B	THR199
B	PRO200
B	ZN301
B	EDO304
B	EDO305
B	HOH492

---

site_id	AC9
Number of Residues	9
Details	BINDING SITE FOR RESIDUE PEG B 303

Chain	Residue
B	HIS164
B	PHE173
B	HOH499
B	HOH573
B	HOH769
C	GLN58
C	HIS161
C	PHE173
C	PRO175

---

site_id	BC1
Number of Residues	8
Details	BINDING SITE FOR RESIDUE EDO B 304

Chain	Residue
B	ASN64
B	HIS66
B	GLN89
B	HIS91
B	V50302
B	EDO305
B	HOH450
B	HOH642

---

site_id	BC2
Number of Residues	6
Details	BINDING SITE FOR RESIDUE EDO B 305

Chain	Residue
B	ASN64
B	LYS69
B	V50302
B	EDO304
B	HOH641
B	HOH648

---

site_id	BC3
Number of Residues	6
Details	BINDING SITE FOR RESIDUE EDO B 306

Chain	Residue
B	ASN71
B	LEU72
B	THR88
B	HOH437
B	HOH445
B	HOH456

---

site_id	BC4
Number of Residues	4
Details	BINDING SITE FOR RESIDUE EDO B 307

Chain	Residue
B	SER83
B	ASP124
B	MET234
B	ASP235

---

site_id	BC5
Number of Residues	4
Details	BINDING SITE FOR RESIDUE EDO B 308

Chain	Residue
B	LYS57
B	GLN58
B	HOH617
C	HIS164

---

site_id	BC6
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN C 301

Chain	Residue
C	HIS91
C	HIS93
C	HIS117
C	V50302

---

site_id	BC7
Number of Residues	16
Details	BINDING SITE FOR RESIDUE V50 C 302

Chain	Residue
C	GLN89
C	HIS91
C	HIS93
C	HIS117
C	VAL119
C	SER133
C	LEU139
C	LEU197
C	THR198
C	THR199
C	PRO200
C	PRO201
C	TRP208
C	ZN301
C	EDO303
C	HOH608

---

site_id	BC8
Number of Residues	7
Details	BINDING SITE FOR RESIDUE EDO C 303

Chain	Residue
C	ASN64
C	HIS66
C	GLN89
C	HIS91
C	V50302
C	HOH609
C	HOH611

---

site_id	BC9
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN D 301

Chain	Residue
D	HIS91
D	HIS93
D	HIS117
D	V50302

---

site_id	CC1
Number of Residues	14
Details	BINDING SITE FOR RESIDUE V50 D 302

Chain	Residue
D	GLN89
D	HIS91
D	HIS93
D	HIS117
D	VAL119
D	SER133
D	LEU197
D	THR198
D	THR199
D	PRO200
D	ZN301
D	EDO304
D	EDO305
D	HOH662

---

site_id	CC2
Number of Residues	9
Details	BINDING SITE FOR RESIDUE PEG D 303

Chain	Residue
D	GLN163
D	GLU220
D	ALA224
D	HOH531
D	HOH551
D	HOH582
D	HOH606
D	HOH626
D	HOH786

---

site_id	CC3
Number of Residues	8
Details	BINDING SITE FOR RESIDUE EDO D 304

Chain	Residue
D	ASN64
D	HIS66
D	SER67
D	GLN89
D	HIS91
D	V50302
D	EDO305
D	HOH664

---

site_id	CC4
Number of Residues	7
Details	BINDING SITE FOR RESIDUE EDO D 305

Chain	Residue
D	ASN64
D	LYS69
D	GLN89
D	V50302
D	EDO304
D	HOH663
D	HOH665

---

site_id	CC5
Number of Residues	8
Details	BINDING SITE FOR RESIDUE EDO D 306

Chain	Residue
A	ALA55
A	PRO175
A	HOH677
A	HOH728
A	HOH729
D	SER160
D	HIS161
D	HIS164

---

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

---