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4ORR

Threedimensional structure of the C65A mutant of Human lipocalin-type Prostaglandin D Synthase olo-form

Functional Information from GO Data
ChainGOidnamespacecontents
A0036094molecular_functionsmall molecule binding
Functional Information from PDB Data
site_idAC1
Number of Residues17
DetailsBINDING SITE FOR RESIDUE PE3 A 401
ChainResidue
ASER45
AGLY140
APHE143
AMET145
ATYR149
AHOH517
AHOH533
AHOH544
AHOH544
ALYS59
ALEU62
AMET64
ASER81
AMET94
ATYR107
ATRP112
ATYR116

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 A 402
ChainResidue
ATRP54
ALYS58
ALYS137
AGLY138
AGLU141

Functional Information from PROSITE/UniProt
site_idPS00213
Number of Residues14
DetailsLIPOCALIN Lipocalin signature. NFQqdKFLGRWFSA
ChainResidueDetails
AASN33-ALA46

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Nucleophile => ECO:0000269|PubMed:20667974
ChainResidueDetails
AALA65

site_idSWS_FT_FI2
Number of Residues1
DetailsCARBOHYD: O-linked (GalNAc...) serine => ECO:0000269|PubMed:23234360
ChainResidueDetails
ASER29

site_idSWS_FT_FI3
Number of Residues1
DetailsCARBOHYD: N-linked (GlcNAc...) (complex) asparagine => ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:19838169, ECO:0000269|PubMed:8336134
ChainResidueDetails
AASN51

site_idSWS_FT_FI4
Number of Residues1
DetailsCARBOHYD: 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
ChainResidueDetails
AASN78

224201

PDB entries from 2024-08-28

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