1K9Z

The PAPase Hal2p complexed with zinc ions

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000103	biological_process	sulfate assimilation
A	0005575	cellular_component	cellular_component
A	0005634	cellular_component	nucleus
A	0005737	cellular_component	cytoplasm
A	0006790	biological_process	sulfur compound metabolic process
A	0008441	molecular_function	3'(2'),5'-bisphosphate nucleotidase activity
A	0009086	biological_process	methionine biosynthetic process
A	0016078	biological_process	tRNA decay
A	0016787	molecular_function	hydrolase activity
A	0016791	molecular_function	phosphatase activity
A	0042538	biological_process	hyperosmotic salinity response
A	0046854	biological_process	phosphatidylinositol phosphate biosynthetic process
A	0046872	molecular_function	metal ion binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	7
Details	BINDING SITE FOR RESIDUE ZN A 401

Chain	Residue
A	GLU72
A	ZN402
A	HOH502
A	HOH503
A	HOH517
A	HOH518
A	HOH793

---

site_id	AC2
Number of Residues	6
Details	BINDING SITE FOR RESIDUE ZN A 402

Chain	Residue
A	ILE144
A	ZN401
A	HOH518
A	HOH794
A	GLU72
A	ASP142

---

site_id	AC3
Number of Residues	6
Details	BINDING SITE FOR RESIDUE ZN A 403

Chain	Residue
A	ASP142
A	ASP145
A	ASP294
A	HOH505
A	HOH511
A	HOH803

---

site_id	AC4
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN A 404

Chain	Residue
A	GLU27
A	GLU89
A	HOH566
A	HOH653

---

site_id	AC5
Number of Residues	5
Details	BINDING SITE FOR RESIDUE ZN A 405

Chain	Residue
A	HIS221
A	HIS224
A	HOH560
A	HOH665
A	HOH668

---

site_id	AC6
Number of Residues	5
Details	BINDING SITE FOR RESIDUE ZN A 406

Chain	Residue
A	GLU235
A	HIS244
A	HIS261
A	HOH613
A	HOH720

---

site_id	AC7
Number of Residues	6
Details	BINDING SITE FOR RESIDUE ZN A 407

Chain	Residue
A	HIS191
A	GLU192
A	ZN408
A	HOH620
A	HOH646
A	HOH729

---

site_id	AC8
Number of Residues	6
Details	BINDING SITE FOR RESIDUE ZN A 408

Chain	Residue
A	GLU131
A	HIS191
A	ZN407
A	HOH522
A	HOH620
A	HOH646

---

site_id	AC9
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN A 409

Chain	Residue
A	ASP315
A	ASP342
A	HOH748
A	HOH786

---

site_id	BC1
Number of Residues	3
Details	BINDING SITE FOR RESIDUE BME A 501

Chain	Residue
A	MET313
A	CYS349
A	GLN353

---

Functional Information from PROSITE/UniProt

site_id	PS00629
Number of Residues	14
Details	IMP_1 Inositol monophosphatase family signature 1. WcLDPIDGTkgFlR

Chain	Residue	Details
A	TRP139-ARG152

---

site_id	PS00630
Number of Residues	15
Details	IMP_2 Inositol monophosphatase family signature 2. WDhAAGnVIVheaGG

Chain	Residue	Details
A	TRP293-GLY307

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	2
Details	ACT_SITE: Proton acceptor => ECO:0000305|PubMed:12126627

Chain	Residue	Details
A	ASP49
A	THR147

---

site_id	SWS_FT_FI2
Number of Residues	2
Details	BINDING: BINDING => ECO:0000269|PubMed:10656801, ECO:0000269|PubMed:12126627, ECO:0007744|PDB:1K9Y, ECO:0007744|PDB:1QGX

Chain	Residue	Details
A	GLU72
A	ILE144

---

site_id	SWS_FT_FI3
Number of Residues	3
Details	BINDING: BINDING => ECO:0000269|PubMed:12126627, ECO:0007744|PDB:1K9Y, ECO:0007744|PDB:1KA1

Chain	Residue	Details
A	ASP145
A	ASP294
A	ASP142

---

site_id	SWS_FT_FI4
Number of Residues	1
Details	BINDING: BINDING => ECO:0000269|PubMed:12126627, ECO:0007744|PDB:1KA1

Chain	Residue	Details
A	THR147

---

site_id	SWS_FT_FI5
Number of Residues	4
Details	BINDING: BINDING => ECO:0000269|PubMed:10656801, ECO:0000269|PubMed:12126627, ECO:0000269|Ref.10, ECO:0007744|PDB:1K9Y, ECO:0007744|PDB:1KA0, ECO:0007744|PDB:1QGX

Chain	Residue	Details
A	HIS241
A	SER264
A	LYS267
A	ARG281

---

Catalytic Information from CSA

site_id	MCSA1
Number of Residues	7
Details	M-CSA 904

Chain	Residue	Details
A	ASP49	proton acceptor, proton donor
A	GLU72	metal ligand
A	ASP142	metal ligand
A	ILE144	metal ligand
A	ASP145	metal ligand
A	THR147	proton acceptor, proton donor, proton relay
A	ASP294	metal ligand

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