2NMM

Crystal structure of human phosphohistidine phosphatase. Northeast Structural Genomics Consortium target HR1409

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004721	molecular_function	phosphoprotein phosphatase activity
A	0004857	molecular_function	enzyme inhibitor activity
A	0005515	molecular_function	protein binding
A	0005737	cellular_component	cytoplasm
A	0005829	cellular_component	cytosol
A	0016787	molecular_function	hydrolase activity
A	0019855	molecular_function	calcium channel inhibitor activity
A	0030036	biological_process	actin cytoskeleton organization
A	0035774	biological_process	positive regulation of insulin secretion involved in cellular response to glucose stimulus
A	0044325	molecular_function	transmembrane transporter binding
A	0050860	biological_process	negative regulation of T cell receptor signaling pathway
A	0051015	molecular_function	actin filament binding
A	0061851	cellular_component	leading edge of lamellipodium
A	0070062	cellular_component	extracellular exosome
A	0097581	biological_process	lamellipodium organization
A	0101006	molecular_function	protein histidine phosphatase activity
A	2000147	biological_process	positive regulation of cell motility
B	0004721	molecular_function	phosphoprotein phosphatase activity
B	0004857	molecular_function	enzyme inhibitor activity
B	0005515	molecular_function	protein binding
B	0005737	cellular_component	cytoplasm
B	0005829	cellular_component	cytosol
B	0016787	molecular_function	hydrolase activity
B	0019855	molecular_function	calcium channel inhibitor activity
B	0030036	biological_process	actin cytoskeleton organization
B	0035774	biological_process	positive regulation of insulin secretion involved in cellular response to glucose stimulus
B	0044325	molecular_function	transmembrane transporter binding
B	0050860	biological_process	negative regulation of T cell receptor signaling pathway
B	0051015	molecular_function	actin filament binding
B	0061851	cellular_component	leading edge of lamellipodium
B	0070062	cellular_component	extracellular exosome
B	0097581	biological_process	lamellipodium organization
B	0101006	molecular_function	protein histidine phosphatase activity
B	2000147	biological_process	positive regulation of cell motility
C	0004721	molecular_function	phosphoprotein phosphatase activity
C	0004857	molecular_function	enzyme inhibitor activity
C	0005515	molecular_function	protein binding
C	0005737	cellular_component	cytoplasm
C	0005829	cellular_component	cytosol
C	0016787	molecular_function	hydrolase activity
C	0019855	molecular_function	calcium channel inhibitor activity
C	0030036	biological_process	actin cytoskeleton organization
C	0035774	biological_process	positive regulation of insulin secretion involved in cellular response to glucose stimulus
C	0044325	molecular_function	transmembrane transporter binding
C	0050860	biological_process	negative regulation of T cell receptor signaling pathway
C	0051015	molecular_function	actin filament binding
C	0061851	cellular_component	leading edge of lamellipodium
C	0070062	cellular_component	extracellular exosome
C	0097581	biological_process	lamellipodium organization
C	0101006	molecular_function	protein histidine phosphatase activity
C	2000147	biological_process	positive regulation of cell motility

Functional Information from PDB Data

site_id	AC1
Number of Residues	9
Details	BINDING SITE FOR RESIDUE SO4 C 201

Chain	Residue
B	ARG78
B	TYR91
C	TYR52
C	HIS53
C	ALA54
C	SER94
C	MSE95
C	ALA96
C	SO4202

---

site_id	AC2
Number of Residues	9
Details	BINDING SITE FOR RESIDUE SO4 C 202

Chain	Residue
B	ARG78
C	LYS21
C	HIS53
C	ARG78
C	TYR93
C	SER94
C	MSE95
C	SO4201
C	HOH203

---

site_id	AC3
Number of Residues	7
Details	BINDING SITE FOR RESIDUE SO4 B 203

Chain	Residue
A	ARG78
B	LYS21
B	HIS53
B	ARG78
B	MSE95
B	SO4206
B	HOH207

---

site_id	AC4
Number of Residues	7
Details	BINDING SITE FOR RESIDUE SO4 A 204

Chain	Residue
A	LYS21
A	HIS53
A	ARG78
A	MSE95
A	SO4205
A	HOH218
C	ARG78

---

site_id	AC5
Number of Residues	9
Details	BINDING SITE FOR RESIDUE SO4 A 205

Chain	Residue
A	TYR52
A	HIS53
A	ALA54
A	SER94
A	MSE95
A	ALA96
A	SO4204
C	ARG78
C	TYR91

---

site_id	AC6
Number of Residues	9
Details	BINDING SITE FOR RESIDUE SO4 B 206

Chain	Residue
A	ARG78
A	TYR91
B	TYR52
B	HIS53
B	ALA54
B	SER94
B	MSE95
B	ALA96
B	SO4203

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	3
Details	Active site: {"description":"Proton acceptor","evidences":[{"source":"PubMed","id":"18991813","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI2
Number of Residues	2
Details	Binding site: {"evidences":[{"source":"PubMed","id":"18991813","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI3
Number of Residues	3
Details	Modified residue: {"description":"N-acetylalanine","evidences":[{"source":"PubMed","id":"19413330","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"22223895","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"22814378","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

Catalytic Information from CSA

site_id	MCSA1
Number of Residues	6
Details	M-CSA 952

Chain	Residue	Details
A	SER29	electrostatic stabiliser, modifies pKa
A	SER61	proton acceptor, proton donor
A	GLY62	electrostatic stabiliser
A	VAL90	electrostatic stabiliser
A	THR106	electrostatic stabiliser
A	LYS112	electrostatic stabiliser

---

site_id	MCSA2
Number of Residues	6
Details	M-CSA 952

Chain	Residue	Details
B	SER29	electrostatic stabiliser, modifies pKa
B	SER61	proton acceptor, proton donor
B	GLY62	electrostatic stabiliser
B	VAL90	electrostatic stabiliser
B	THR106	electrostatic stabiliser
B	LYS112	electrostatic stabiliser

---

site_id	MCSA3
Number of Residues	5
Details	M-CSA 952

Chain	Residue	Details
C	SER61	proton acceptor, proton donor
C	GLY62	electrostatic stabiliser
C	VAL90	electrostatic stabiliser
C	THR106	electrostatic stabiliser
C	LYS112	electrostatic stabiliser

---