4JOD

Crystal structure of human lysophosphatidic acid phosphatase type 6 complexed with Tris

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0002244	biological_process	hematopoietic progenitor cell differentiation
A	0003993	molecular_function	acid phosphatase activity
A	0005737	cellular_component	cytoplasm
A	0005739	cellular_component	mitochondrion
A	0005759	cellular_component	mitochondrial matrix
A	0006629	biological_process	lipid metabolic process
A	0006644	biological_process	phospholipid metabolic process
A	0006654	biological_process	phosphatidic acid biosynthetic process
A	0016787	molecular_function	hydrolase activity
A	0052642	molecular_function	lysophosphatidic acid phosphatase activity
A	2001311	biological_process	lysobisphosphatidic acid metabolic process

Functional Information from PDB Data

site_id	AC1
Number of Residues	7
Details	BINDING SITE FOR RESIDUE TRS A 501

Chain	Residue
A	ARG58
A	HIS59
A	ARG62
A	ARG168
A	HIS334
A	ASP335
A	HOH735

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Functional Information from PROSITE/UniProt

site_id	PS00616
Number of Residues	15
Details	HIS_ACID_PHOSPHAT_1 Histidine acid phosphatases phosphohistidine signature. LkmVqvVfRHGaRsP

Chain	Residue	Details
A	LEU50-PRO64

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	110
Details	Region: {"description":"Substrate binding","evidences":[{"evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI2
Number of Residues	1
Details	Active site: {"description":"Nucleophile","evidences":[{"source":"PubMed","id":"23807634","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI3
Number of Residues	1
Details	Active site: {"description":"Proton donor","evidences":[{"source":"PubMed","id":"23807634","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

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