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3CJ7

Structure of Rattus norvegicus NTPDase2 in complex with AMP

Functional Information from GO Data
ChainGOidnamespacecontents
A0016787molecular_functionhydrolase activity
Functional Information from PDB Data
site_idAC1
Number of Residues14
DetailsBINDING SITE FOR RESIDUE AMP A 501
ChainResidue
ASER48
ATYR398
AHOH508
AHOH509
AHOH649
AHOH699
ASER49
AHIS50
AGLY203
AGLY204
AARG245
AASP246
ATYR350
AARG394

Functional Information from PROSITE/UniProt
site_idPS01238
Number of Residues16
DetailsGDA1_CD39_NTPASE GDA1/CD39 family of nucleoside phosphatases signature. LsGqdEGvFgWVTaNY
ChainResidueDetails
ALEU160-TYR175

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsActive site: {"description":"Proton acceptor","evidences":[{"source":"PubMed","id":"18458329","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues4
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"18458329","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues1
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"24090084","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues5
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

246704

PDB entries from 2025-12-24

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