4ORU

Three-dimensional structure of the C65A mutant of Human lipocalin-type Prostaglandin D Synthase holo-form second space group

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0036094	molecular_function	small molecule binding
B	0036094	molecular_function	small molecule binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	32
Details	BINDING SITE FOR RESIDUE PEU A 201

Chain	Residue
A	ASN51
A	SER133
A	ASP142
A	PHE143
A	MET145
A	THR147
A	TYR149
A	HOH314
B	ASN51
B	LEU55
B	LYS59
A	SER52
B	LEU62
B	MET64
B	SER81
B	PHE83
B	MET94
B	TYR107
B	TRP112
B	SER133
B	ASP142
B	MET145
A	LEU55
B	TYR149
B	HOH210
B	HOH224
A	LYS59
A	LEU62
A	SER81
A	PHE83
A	MET94
A	TYR116

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Functional Information from PROSITE/UniProt

site_id	PS00213
Number of Residues	14
Details	LIPOCALIN Lipocalin signature. NFQqdKFLGRWFSA

Chain	Residue	Details
A	ASN33-ALA46

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	2
Details	ACT_SITE: Nucleophile => ECO:0000269|PubMed:20667974

Chain	Residue	Details
A	ALA65
B	ALA65

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site_id	SWS_FT_FI2
Number of Residues	2
Details	CARBOHYD: O-linked (GalNAc...) serine => ECO:0000269|PubMed:23234360

Chain	Residue	Details
A	SER29
B	SER29

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site_id	SWS_FT_FI3
Number of Residues	2
Details	CARBOHYD: N-linked (GlcNAc...) (complex) asparagine => ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:19838169, ECO:0000269|PubMed:8336134

Chain	Residue	Details
A	ASN51
B	ASN51

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site_id	SWS_FT_FI4
Number of Residues	2
Details	CARBOHYD: N-linked (GlcNAc...) (complex) asparagine => ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:19139490, ECO:0000269|PubMed:19838169, ECO:0000269|PubMed:22171320, ECO:0000269|PubMed:8336134

Chain	Residue	Details
A	ASN78
B	ASN78

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