Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

2A8D

Haemophilus influenzae beta-carbonic anhydrase complexed with bicarbonate

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004089	molecular_function	carbonate dehydratase activity
A	0005575	cellular_component	cellular_component
A	0008270	molecular_function	zinc ion binding
A	0015976	biological_process	carbon utilization
A	0016829	molecular_function	lyase activity
A	0046872	molecular_function	metal ion binding
B	0004089	molecular_function	carbonate dehydratase activity
B	0005575	cellular_component	cellular_component
B	0008270	molecular_function	zinc ion binding
B	0015976	biological_process	carbon utilization
B	0016829	molecular_function	lyase activity
B	0046872	molecular_function	metal ion binding
C	0004089	molecular_function	carbonate dehydratase activity
C	0005575	cellular_component	cellular_component
C	0008270	molecular_function	zinc ion binding
C	0015976	biological_process	carbon utilization
C	0016829	molecular_function	lyase activity
C	0046872	molecular_function	metal ion binding
D	0004089	molecular_function	carbonate dehydratase activity
D	0005575	cellular_component	cellular_component
D	0008270	molecular_function	zinc ion binding
D	0015976	biological_process	carbon utilization
D	0016829	molecular_function	lyase activity
D	0046872	molecular_function	metal ion binding
E	0004089	molecular_function	carbonate dehydratase activity
E	0005575	cellular_component	cellular_component
E	0008270	molecular_function	zinc ion binding
E	0015976	biological_process	carbon utilization
E	0016829	molecular_function	lyase activity
E	0046872	molecular_function	metal ion binding
F	0004089	molecular_function	carbonate dehydratase activity
F	0005575	cellular_component	cellular_component
F	0008270	molecular_function	zinc ion binding
F	0015976	biological_process	carbon utilization
F	0016829	molecular_function	lyase activity
F	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 1230

Chain	Residue
A	CYS42
A	ASP44
A	HIS98
A	CYS101

site_id	AC2
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN B 2230

Chain	Residue
B	CYS42
B	ASP44
B	HIS98
B	CYS101

site_id	AC3
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN C 3230

Chain	Residue
C	ASP44
C	HIS98
C	CYS101
C	CYS42

site_id	AC4
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN D 4230

Chain	Residue
D	CYS42
D	ASP44
D	HIS98
D	CYS101

site_id	AC5
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN E 5230

Chain	Residue
E	CYS42
E	ASP44
E	HIS98
E	CYS101

site_id	AC6
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN F 6230

Chain	Residue
F	CYS42
F	ASP44
F	HIS98
F	CYS101

site_id	AC7
Number of Residues	9
Details	BINDING SITE FOR RESIDUE BCT A 1001

Chain	Residue
A	TRP39
A	GLY41
A	VAL47
A	PRO48
A	ALA49
A	ARG64
A	TYR181
A	HOH1233
A	HOH1239

site_id	AC8
Number of Residues	9
Details	BINDING SITE FOR RESIDUE BCT B 1002

Chain	Residue
B	TRP39
B	GLY41
B	VAL47
B	ALA49
B	LEU52
B	ARG64
B	TYR181
B	HOH2247
B	HOH2248

site_id	AC9
Number of Residues	9
Details	BINDING SITE FOR RESIDUE BCT C 1003

Chain	Residue
C	TRP39
C	GLY41
C	VAL47
C	ALA49
C	LEU52
C	ARG64
C	TYR181
C	HOH3233
C	HOH3242

site_id	BC1
Number of Residues	9
Details	BINDING SITE FOR RESIDUE BCT D 1004

Chain	Residue
D	TRP39
D	GLY41
D	VAL47
D	PRO48
D	ALA49
D	ARG64
D	TYR181
D	HOH4233
D	HOH4236

site_id	BC2
Number of Residues	9
Details	BINDING SITE FOR RESIDUE BCT E 1005

Chain	Residue
E	TRP39
E	GLY41
E	VAL47
E	PRO48
E	ALA49
E	ARG64
E	TYR181
E	HOH5244
E	HOH5261

site_id	BC3
Number of Residues	7
Details	BINDING SITE FOR RESIDUE BCT F 1006

Chain	Residue
F	TRP39
F	VAL47
F	ALA49
F	ARG64
F	TYR181
F	HOH6233
F	HOH6234

site_id	BC4
Number of Residues	5
Details	BINDING SITE FOR RESIDUE SO4 B 2001

Chain	Residue
A	ARG160
A	LYS165
A	ARG198
B	LEU121
B	ARG124

site_id	BC5
Number of Residues	5
Details	BINDING SITE FOR RESIDUE SO4 B 2002

Chain	Residue
A	ARG124
A	PHE128
B	ARG160
B	ARG198
B	HOH2243

site_id	BC6
Number of Residues	4
Details	BINDING SITE FOR RESIDUE SO4 C 2003

Chain	Residue
C	ARG160
C	ARG198
C	HOH3240
D	ARG124

site_id	BC7
Number of Residues	4
Details	BINDING SITE FOR RESIDUE SO4 D 2004

Chain	Residue
C	ARG124
D	ARG160
D	ARG198
D	HOH4245

site_id	BC8
Number of Residues	5
Details	BINDING SITE FOR RESIDUE SO4 E 2005

Chain	Residue
E	ARG160
E	LYS165
E	ARG198
E	HOH5236
F	ARG124

site_id	BC9
Number of Residues	6
Details	BINDING SITE FOR RESIDUE SO4 E 2006

Chain	Residue
E	LEU121
E	ARG124
E	PHE128
E	HOH5237
F	ARG160
F	ARG198

Functional Information from PROSITE/UniProt

site_id	PS00704
Number of Residues	8
Details	PROK_CO2_ANHYDRASE_1 Prokaryotic-type carbonic anhydrases signature 1. CSDSRVpA

Chain	Residue	Details
A	CYS42-ALA49

site_id	PS00705
Number of Residues	21
Details	PROK_CO2_ANHYDRASE_2 Prokaryotic-type carbonic anhydrases signature 2. QYAVdvLkiehIIIcGHtnCG

Chain	Residue	Details
A	GLN82-GLY102

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	24
Details	BINDING: BINDING => ECO:0000269\|PubMed:16584170, ECO:0007744\|PDB:2A8C, ECO:0007744\|PDB:2A8D

Chain	Residue	Details
A	CYS42
C	ASP44
C	HIS98
C	CYS101
D	CYS42
D	ASP44
D	HIS98
D	CYS101
E	CYS42
E	ASP44
E	HIS98
A	ASP44
E	CYS101
F	CYS42
F	ASP44
F	HIS98
F	CYS101
A	HIS98
A	CYS101
B	CYS42
B	ASP44
B	HIS98
B	CYS101
C	CYS42

Catalytic Information from CSA

site_id	CSA1
Number of Residues	2
Details	Annotated By Reference To The Literature 1i6p

Chain	Residue	Details
A	ASP44
A	ARG46

site_id	CSA2
Number of Residues	2
Details	Annotated By Reference To The Literature 1i6p

Chain	Residue	Details
B	ASP44
B	ARG46

site_id	CSA3
Number of Residues	2
Details	Annotated By Reference To The Literature 1i6p

Chain	Residue	Details
C	ASP44
C	ARG46

site_id	CSA4
Number of Residues	2
Details	Annotated By Reference To The Literature 1i6p

Chain	Residue	Details
D	ASP44
D	ARG46

site_id	CSA5
Number of Residues	2
Details	Annotated By Reference To The Literature 1i6p

Chain	Residue	Details
E	ASP44
E	ARG46

site_id	CSA6
Number of Residues	2
Details	Annotated By Reference To The Literature 1i6p

Chain	Residue	Details
F	ASP44
F	ARG46

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		PDB format (full)
		Validation report (PDF)
		EDMap 2fo-fc (MTZ)