6HWR

Red kidney bean purple acid phosphatase in complex with adenosine divanadate

Replaces:  4KKZ

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0003993	molecular_function	acid phosphatase activity
A	0005576	cellular_component	extracellular region
A	0008199	molecular_function	ferric iron binding
A	0008270	molecular_function	zinc ion binding
A	0016787	molecular_function	hydrolase activity
A	0046872	molecular_function	metal ion binding
B	0003993	molecular_function	acid phosphatase activity
B	0005576	cellular_component	extracellular region
B	0008199	molecular_function	ferric iron binding
B	0008270	molecular_function	zinc ion binding
B	0016787	molecular_function	hydrolase activity
B	0046872	molecular_function	metal ion binding
C	0003993	molecular_function	acid phosphatase activity
C	0005576	cellular_component	extracellular region
C	0008199	molecular_function	ferric iron binding
C	0008270	molecular_function	zinc ion binding
C	0016787	molecular_function	hydrolase activity
C	0046872	molecular_function	metal ion binding
D	0003993	molecular_function	acid phosphatase activity
D	0005576	cellular_component	extracellular region
D	0008199	molecular_function	ferric iron binding
D	0008270	molecular_function	zinc ion binding
D	0016787	molecular_function	hydrolase activity
D	0046872	molecular_function	metal ion binding

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	1
Details	ACT_SITE: Proton donor => ECO:0000303|PubMed:7770774, ECO:0000303|PubMed:8683579

Chain	Residue	Details
D	HIS296
B	HIS296
A	HIS296

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site_id	SWS_FT_FI2
Number of Residues	7
Details	BINDING: BINDING => ECO:0000269|PubMed:22943065, ECO:0000269|PubMed:8683579

Chain	Residue	Details
D	ASP135
B	TYR167
B	ASN201
B	HIS286
B	HIS323
B	HIS325
A	ASP135
A	ASP164
A	TYR167
A	ASN201
A	HIS286
D	ASP164
A	HIS323
A	HIS325
D	TYR167
D	ASN201
D	HIS286
D	HIS323
D	HIS325
B	ASP135
B	ASP164

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site_id	SWS_FT_FI3
Number of Residues	1
Details	CARBOHYD: N-linked (GlcNAc...) asparagine; partial => ECO:0000269|PubMed:22943065, ECO:0000269|PubMed:8125089, ECO:0000269|PubMed:8683579

Chain	Residue	Details
D	ASN81
B	ASN81
A	ASN81

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site_id	SWS_FT_FI4
Number of Residues	3
Details	CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:22943065, ECO:0000269|PubMed:8125089, ECO:0000269|PubMed:8683579

Chain	Residue	Details
D	ASN109
D	ASN143
D	ASN396
B	ASN109
B	ASN143
B	ASN396
A	ASN109
A	ASN143
A	ASN396

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site_id	SWS_FT_FI5
Number of Residues	1
Details	CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:8125089, ECO:0000269|PubMed:8683579

Chain	Residue	Details
D	ASN211
B	ASN211
A	ASN211

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Catalytic Information from CSA

site_id	MCSA1
Number of Residues	10
Details	M-CSA 43

Chain	Residue	Details
D	ASP135	metal ligand
D	HIS325	metal ligand
D	ASP164	metal ligand
D	TYR167	metal ligand
D	ASN201	metal ligand
D	HIS202	electrostatic stabiliser, hydrogen bond donor
D	HIS286	metal ligand
D	HIS295	electrostatic stabiliser, hydrogen bond donor
D	HIS296	electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton donor
D	HIS323	metal ligand

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site_id	MCSA2
Number of Residues	10
Details	M-CSA 43

Chain	Residue	Details
B	ASP135	metal ligand
B	HIS325	metal ligand
B	ASP164	metal ligand
B	TYR167	metal ligand
B	ASN201	metal ligand
B	HIS202	electrostatic stabiliser, hydrogen bond donor
B	HIS286	metal ligand
B	HIS295	electrostatic stabiliser, hydrogen bond donor
B	HIS296	electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton donor
B	HIS323	metal ligand

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site_id	MCSA3
Number of Residues	10
Details	M-CSA 43

Chain	Residue	Details
A	ASP135	metal ligand
A	HIS325	metal ligand
A	ASP164	metal ligand
A	TYR167	metal ligand
A	ASN201	metal ligand
A	HIS202	electrostatic stabiliser, hydrogen bond donor
A	HIS286	metal ligand
A	HIS295	electrostatic stabiliser, hydrogen bond donor
A	HIS296	electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton donor
A	HIS323	metal ligand

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