Loading
PDBj
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDBDonate
RCSB PDBPDBeBMRBAdv. SearchSearch help

4KJD

RatIntestinal AP expressed in E. coli

Functional Information from GO Data
ChainGOidnamespacecontents
A0000287molecular_functionmagnesium ion binding
A0002020molecular_functionprotease binding
A0004035molecular_functionalkaline phosphatase activity
A0005515molecular_functionprotein binding
A0005886cellular_componentplasma membrane
A0008270molecular_functionzinc ion binding
A0009897cellular_componentexternal side of plasma membrane
A0016311biological_processdephosphorylation
A0016787molecular_functionhydrolase activity
A0016791molecular_functionphosphatase activity
A0042803molecular_functionprotein homodimerization activity
A0046872molecular_functionmetal ion binding
A0071773biological_processcellular response to BMP stimulus
A0098552cellular_componentside of membrane
B0000287molecular_functionmagnesium ion binding
B0002020molecular_functionprotease binding
B0004035molecular_functionalkaline phosphatase activity
B0005515molecular_functionprotein binding
B0005886cellular_componentplasma membrane
B0008270molecular_functionzinc ion binding
B0009897cellular_componentexternal side of plasma membrane
B0016311biological_processdephosphorylation
B0016787molecular_functionhydrolase activity
B0016791molecular_functionphosphatase activity
B0042803molecular_functionprotein homodimerization activity
B0046872molecular_functionmetal ion binding
B0071773biological_processcellular response to BMP stimulus
B0098552cellular_componentside of membrane
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MG A 501
ChainResidue
ASER155
AGLU311
AHOH734
AHOH735
AHOH736
AHOH737

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MG A 502
ChainResidue
AASP285
AHOH634
AGLU216
APHE269
AGLU270

site_idAC3
Number of Residues8
DetailsBINDING SITE FOR RESIDUE GOL A 503
ChainResidue
ALYS34
AASN35
ASER300
ATHR345
AASN346
AASP349
ATHR350
AHOH651

site_idAC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MG B 501
ChainResidue
BSER155
BGLU311
BHOH704
BHOH737
BHOH738
BHOH739

site_idAC5
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MG B 502
ChainResidue
BGLU216
BPHE269
BGLU270
BASP285
BHOH609

site_idAC6
Number of Residues7
DetailsBINDING SITE FOR RESIDUE GOL B 503
ChainResidue
BLYS34
BASN35
BSER300
BASN346
BASP349
BTHR350
BHOH631

Functional Information from PROSITE/UniProt
site_idPS00123
Number of Residues9
DetailsALKALINE_PHOSPHATASE Alkaline phosphatase active site. VpDSAGTAT
ChainResidueDetails
AVAL89-THR97

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsActive site: {"description":"Phosphoserine intermediate","evidences":[{"source":"PROSITE-ProRule","id":"PRU10042","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"24076154","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues14
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"24076154","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues8
DetailsBinding site: {"evidences":[{"source":"UniProtKB","id":"P05186","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues2
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues2
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"24076154","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

242199

PDB entries from 2025-09-24

PDB statisticsPDBj update infoContact PDBjnumon