Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

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	0005515	molecular_function	protein binding
A	0005654	cellular_component	nucleoplasm
A	0005737	cellular_component	cytoplasm
A	0005829	cellular_component	cytosol
A	0005886	cellular_component	plasma membrane
A	0006470	biological_process	protein dephosphorylation
A	0016604	cellular_component	nuclear body
A	0019855	molecular_function	calcium channel inhibitor activity
A	0030036	biological_process	actin cytoskeleton organization
A	0035971	biological_process	peptidyl-histidine dephosphorylation
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	0051350	biological_process	negative regulation of lyase activity
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
A	2000984	biological_process	negative regulation of ATP citrate synthase activity
B	0004721	molecular_function	phosphoprotein phosphatase activity
B	0005515	molecular_function	protein binding
B	0005654	cellular_component	nucleoplasm
B	0005737	cellular_component	cytoplasm
B	0005829	cellular_component	cytosol
B	0005886	cellular_component	plasma membrane
B	0006470	biological_process	protein dephosphorylation
B	0016604	cellular_component	nuclear body
B	0019855	molecular_function	calcium channel inhibitor activity
B	0030036	biological_process	actin cytoskeleton organization
B	0035971	biological_process	peptidyl-histidine dephosphorylation
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	0051350	biological_process	negative regulation of lyase activity
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
B	2000984	biological_process	negative regulation of ATP citrate synthase activity
C	0004721	molecular_function	phosphoprotein phosphatase activity
C	0005515	molecular_function	protein binding
C	0005654	cellular_component	nucleoplasm
C	0005737	cellular_component	cytoplasm
C	0005829	cellular_component	cytosol
C	0005886	cellular_component	plasma membrane
C	0006470	biological_process	protein dephosphorylation
C	0016604	cellular_component	nuclear body
C	0019855	molecular_function	calcium channel inhibitor activity
C	0030036	biological_process	actin cytoskeleton organization
C	0035971	biological_process	peptidyl-histidine dephosphorylation
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	0051350	biological_process	negative regulation of lyase activity
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
C	2000984	biological_process	negative regulation of ATP citrate synthase activity

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	ACT_SITE: Proton acceptor => ECO:0000269\|PubMed:18991813

Chain	Residue	Details
A	HIS53
B	HIS53
C	HIS53

site_id	SWS_FT_FI2
Number of Residues	6
Details	BINDING: BINDING => ECO:0000305\|PubMed:18991813

Chain	Residue	Details
A	LYS21
A	SER94
B	LYS21
B	SER94
C	LYS21
C	SER94

site_id	SWS_FT_FI3
Number of Residues	3
Details	MOD_RES: N-acetylalanine => ECO:0007744\|PubMed:19413330, ECO:0007744\|PubMed:22223895, ECO:0007744\|PubMed:22814378

Chain	Residue	Details
A	ALA2
B	ALA2
C	ALA2

Catalytic Information from CSA

site_id	MCSA1
Number of Residues	6
Details	M-CSA 952

Chain	Residue	Details
A	LYS21	electrostatic stabiliser, modifies pKa
A	HIS53	proton acceptor, proton donor
A	ALA54	electrostatic stabiliser
A	ARG78	electrostatic stabiliser
A	SER94	electrostatic stabiliser
A	ALA96	electrostatic stabiliser

site_id	MCSA2
Number of Residues	6
Details	M-CSA 952

Chain	Residue	Details
B	LYS21	electrostatic stabiliser, modifies pKa
B	HIS53	proton acceptor, proton donor
B	ALA54	electrostatic stabiliser
B	ARG78	electrostatic stabiliser
B	SER94	electrostatic stabiliser
B	ALA96	electrostatic stabiliser

site_id	MCSA3
Number of Residues	6
Details	M-CSA 952

Chain	Residue	Details
C	LYS21	electrostatic stabiliser, modifies pKa
C	HIS53	proton acceptor, proton donor
C	ALA54	electrostatic stabiliser
C	ARG78	electrostatic stabiliser
C	SER94	electrostatic stabiliser
C	ALA96	electrostatic stabiliser

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