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Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

4KBP

KIDNEY BEAN PURPLE ACID PHOSPHATASE

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 PDB Data

site_id	ACA
Number of Residues	2
Details	PHOSPHATASE ACTIVE SITE.

Chain	Residue
A	FE438
A	ZN439

site_id	ACB
Number of Residues	2
Details	PHOSPHATASE ACTIVE SITE.

Chain	Residue
B	FE438
B	ZN439

site_id	ACC
Number of Residues	2
Details	PHOSPHATASE ACTIVE SITE.

Chain	Residue
C	FE438
C	ZN439

site_id	ACD
Number of Residues	2
Details	PHOSPHATASE ACTIVE SITE.

Chain	Residue
D	FE438
D	ZN439

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	4
Details	ACT_SITE: Proton donor => ECO:0000303\|PubMed:7770774, ECO:0000303\|PubMed:8683579

Chain	Residue	Details
A	HIS323
B	HIS323
C	HIS323
D	HIS323

site_id	SWS_FT_FI2
Number of Residues	28
Details	BINDING: BINDING => ECO:0000269\|PubMed:22943065, ECO:0000269\|PubMed:8683579

Chain	Residue	Details
A	VAL162
B	PRO194
B	GLU228
B	LYS313
B	ASP350
B	SER352
C	VAL162
C	ALA191
C	PRO194
C	GLU228
C	LYS313
A	ALA191
C	ASP350
C	SER352
D	VAL162
D	ALA191
D	PRO194
D	GLU228
D	LYS313
D	ASP350
D	SER352
A	PRO194
A	GLU228
A	LYS313
A	ASP350
A	SER352
B	VAL162
B	ALA191

site_id	SWS_FT_FI3
Number of Residues	4
Details	MOD_RES: Blocked amino end (Gly) => ECO:0000269\|PubMed:12054466

Chain	Residue	Details
A	GLY23
B	GLY23
C	GLY23
D	GLY23

site_id	SWS_FT_FI4
Number of Residues	4
Details	CARBOHYD: N-linked (GlcNAc...) asparagine; partial => ECO:0000269\|PubMed:22943065, ECO:0000269\|PubMed:8125089, ECO:0000269\|PubMed:8683579

Chain	Residue	Details
A	ARG108
B	ARG108
C	ARG108
D	ARG108

site_id	SWS_FT_FI5
Number of Residues	12
Details	CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269\|PubMed:22943065, ECO:0000269\|PubMed:8125089, ECO:0000269\|PubMed:8683579

Chain	Residue	Details
A	LEU136
D	LEU136
D	ARG170
D	ARG423
A	ARG170
A	ARG423
B	LEU136
B	ARG170
B	ARG423
C	LEU136
C	ARG170
C	ARG423

site_id	SWS_FT_FI6
Number of Residues	4
Details	CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269\|PubMed:8125089, ECO:0000269\|PubMed:8683579

Chain	Residue	Details
A	TYR238
B	TYR238
C	TYR238
D	TYR238

Catalytic Information from CSA

site_id	CSA1
Number of Residues	3
Details	a catalytic site defined by CSA, PubMed 8683579

Chain	Residue	Details
A	HIS296
A	HIS202
A	HIS295

site_id	CSA2
Number of Residues	3
Details	a catalytic site defined by CSA, PubMed 8683579

Chain	Residue	Details
B	HIS296
B	HIS202
B	HIS295

site_id	CSA3
Number of Residues	3
Details	a catalytic site defined by CSA, PubMed 8683579

Chain	Residue	Details
C	HIS296
C	HIS202
C	HIS295

site_id	CSA4
Number of Residues	3
Details	a catalytic site defined by CSA, PubMed 8683579

Chain	Residue	Details
D	HIS296
D	HIS202
D	HIS295

site_id	MCSA1
Number of Residues	10
Details	M-CSA 43

Chain	Residue	Details
A	VAL162	metal ligand
A	SER352	metal ligand
A	ALA191	metal ligand
A	PRO194	metal ligand
A	GLU228	metal ligand
A	ALA229	electrostatic stabiliser, hydrogen bond donor
A	LYS313	metal ligand
A	GLY322	electrostatic stabiliser, hydrogen bond donor
A	HIS323	electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton donor
A	ASP350	metal ligand

site_id	MCSA2
Number of Residues	10
Details	M-CSA 43

Chain	Residue	Details
B	VAL162	metal ligand
B	SER352	metal ligand
B	ALA191	metal ligand
B	PRO194	metal ligand
B	GLU228	metal ligand
B	ALA229	electrostatic stabiliser, hydrogen bond donor
B	LYS313	metal ligand
B	GLY322	electrostatic stabiliser, hydrogen bond donor
B	HIS323	electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton donor
B	ASP350	metal ligand

site_id	MCSA3
Number of Residues	10
Details	M-CSA 43

Chain	Residue	Details
C	VAL162	metal ligand
C	SER352	metal ligand
C	ALA191	metal ligand
C	PRO194	metal ligand
C	GLU228	metal ligand
C	ALA229	electrostatic stabiliser, hydrogen bond donor
C	LYS313	metal ligand
C	GLY322	electrostatic stabiliser, hydrogen bond donor
C	HIS323	electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton donor
C	ASP350	metal ligand

site_id	MCSA4
Number of Residues	10
Details	M-CSA 43

Chain	Residue	Details
D	VAL162	metal ligand
D	SER352	metal ligand
D	ALA191	metal ligand
D	PRO194	metal ligand
D	GLU228	metal ligand
D	ALA229	electrostatic stabiliser, hydrogen bond donor
D	LYS313	metal ligand
D	GLY322	electrostatic stabiliser, hydrogen bond donor
D	HIS323	electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton donor
D	ASP350	metal ligand

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PDB entries from 2024-07-17

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