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Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

5MSA

Crystal structure of human carbonic anhydrase isozyme XII with 2,3,5,6-Tetrafluoro-4-(propylthio)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	3TV302

site_id	AC2
Number of Residues	17
Details	binding site for residue 3TV A 302

Chain	Residue
A	VAL141
A	LEU197
A	THR198
A	THR199
A	PRO200
A	TRP208
A	ZN301
A	HOH428
A	HOH681
A	HOH702
A	HOH745
A	HOH775
A	HIS91
A	HIS93
A	HIS117
A	VAL119
A	LEU139

site_id	AC3
Number of Residues	6
Details	binding site for residue EDO A 303

Chain	Residue
A	ASN71
A	LEU72
A	THR88
A	HOH419
A	HOH450
A	HOH488

site_id	AC4
Number of Residues	5
Details	binding site for residue EDO A 304

Chain	Residue
A	THR62
A	ASN63
A	ASN64
A	GLY169
A	GLU171

site_id	AC5
Number of Residues	3
Details	binding site for residue EDO A 305

Chain	Residue
A	ASP156
A	SER160
A	HOH423

site_id	AC6
Number of Residues	4
Details	binding site for residue PEG A 306

Chain	Residue
A	SER150
A	PHE151
A	HOH421
A	HOH451

site_id	AC7
Number of Residues	8
Details	binding site for residue EDO A 307

Chain	Residue
A	ASP31
A	HIS33
A	SER108
A	GLY109
A	HOH447
A	HOH656
B	GLY109
B	HIS111

site_id	AC8
Number of Residues	5
Details	binding site for residue EDO A 308

Chain	Residue
A	TYR39
A	ALA41
A	SER260
A	HOH406
A	HOH522

site_id	AC9
Number of Residues	9
Details	binding site for residue EDO A 309

Chain	Residue
A	LEU53
A	SER54
A	LYS57
A	PHE59
A	PRO73
A	ASP75
A	HOH407
A	HOH425
B	GLN49

site_id	AD1
Number of Residues	4
Details	binding site for residue EDO A 310

Chain	Residue
A	ALA224
A	THR227
A	HOH492
A	HOH619

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

Chain	Residue
B	HIS91
B	HIS93
B	HIS117
B	3TV302

site_id	AD3
Number of Residues	18
Details	binding site for residue 3TV B 302

Chain	Residue
B	GLN89
B	HIS91
B	HIS93
B	HIS117
B	VAL119
B	ALA129
B	SER133
B	LEU139
B	VAL141
B	LEU197
B	THR198
B	THR199
B	PRO200
B	TRP208
B	ZN301
B	CIT305
B	HOH422
B	HOH669

site_id	AD4
Number of Residues	8
Details	binding site for residue EDO B 303

Chain	Residue
B	LEU43
B	THR44
B	LEU46
B	GLY80
B	TYR190
B	ARG192
B	HOH469
B	HOH555

site_id	AD5
Number of Residues	4
Details	binding site for residue PEG B 304

Chain	Residue
B	PHE151
B	PRO153
B	HOH461
B	HOH663

site_id	AD6
Number of Residues	10
Details	binding site for residue CIT B 305

Chain	Residue
B	ASN64
B	LYS69
B	GLN89
B	3TV302
B	HOH402
B	HOH406
B	HOH408
B	HOH411
B	HOH422
B	HOH439

site_id	AD7
Number of Residues	4
Details	binding site for residue ZN C 301

Chain	Residue
C	HIS91
C	HIS93
C	HIS117
C	3TV302

site_id	AD8
Number of Residues	14
Details	binding site for residue 3TV C 302

Chain	Residue
C	HIS91
C	HIS93
C	HIS117
C	VAL119
C	ALA129
C	LEU139
C	VAL141
C	LEU197
C	THR198
C	THR199
C	TRP208
C	ZN301
C	HOH632
C	HOH669

site_id	AD9
Number of Residues	6
Details	binding site for residue EDO C 303

Chain	Residue
C	ASN71
C	LEU72
C	THR88
C	HOH444
C	HOH465
C	HOH494

site_id	AE1
Number of Residues	3
Details	binding site for residue PEG C 304

Chain	Residue
C	LYS17
C	LYS18
C	PRO20

site_id	AE2
Number of Residues	8
Details	binding site for residue EDO C 305

Chain	Residue
A	GLN82
C	GLU220
C	LEU223
C	ALA224
C	THR227
C	HOH421
C	HOH426
C	HOH428

site_id	AE3
Number of Residues	4
Details	binding site for residue ZN D 301

Chain	Residue
D	HIS91
D	HIS93
D	HIS117
D	3TV302

site_id	AE4
Number of Residues	17
Details	binding site for residue 3TV D 302

Chain	Residue
D	GLN89
D	HIS91
D	HIS93
D	HIS117
D	VAL119
D	SER133
D	LEU139
D	VAL141
D	LEU197
D	THR198
D	THR199
D	PRO200
D	TRP208
D	ZN301
D	CIT306
D	HOH473
D	HOH488

site_id	AE5
Number of Residues	5
Details	binding site for residue PEG D 303

Chain	Residue
D	THR62
D	LYS168
D	GLY169
D	HIS233
D	HOH463

site_id	AE6
Number of Residues	8
Details	binding site for residue CIT D 304

Chain	Residue
D	SER133
D	ASN134
D	PRO201
D	ASN203
D	HOH401
D	HOH404
D	HOH414
D	HOH488

site_id	AE7
Number of Residues	1
Details	binding site for residue EDO D 305

Chain	Residue
D	ASP235

site_id	AE8
Number of Residues	10
Details	binding site for residue CIT D 306

Chain	Residue
D	ASN64
D	LYS69
D	GLN89
D	3TV302
D	HOH405
D	HOH419
D	HOH447
D	HOH463
D	HOH481
D	HOH650

site_id	AE9
Number of Residues	6
Details	binding site for residue EDO D 307

Chain	Residue
A	GLU171
A	PHE173
D	HIS164
D	ALA172
D	PHE173
D	HOH472

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
A	HIS93
A	HIS117
B	HIS91
B	HIS93
B	HIS117
C	HIS91
C	HIS93
C	HIS117
D	HIS91
D	HIS93
D	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

219869

PDB entries from 2024-05-15

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