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3RO7

Crystal Structure of Mouse Apolipoprotein A-I Binding Protein in Complex with Thymine.

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0002040biological_processsprouting angiogenesis
A0005576cellular_componentextracellular region
A0005615cellular_componentextracellular space
A0005634cellular_componentnucleus
A0005739cellular_componentmitochondrion
A0005829cellular_componentcytosol
A0005929cellular_componentcilium
A0006869biological_processlipid transport
A0010874biological_processregulation of cholesterol efflux
A0016525biological_processnegative regulation of angiogenesis
A0016853molecular_functionisomerase activity
A0031580biological_processmembrane raft distribution
A0042802molecular_functionidentical protein binding
A0044297cellular_componentcell body
A0046496biological_processnicotinamide nucleotide metabolic process
A0046872molecular_functionmetal ion binding
A0052856molecular_functionNAD(P)HX epimerase activity
A0110051biological_processmetabolite repair
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE TDR A 300
ChainResidue
AALA35
AASP39
AASP188
ALEU211
ALYS215

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE SO4 A 301
ChainResidue
ASER161
AHOH286
AGLY88
AASN89
AASN90
AGLY159

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues6
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_03159
ChainResidueDetails
AASN89
AASN90
AASP155
AGLY159
AASP188
ASER191

site_idSWS_FT_FI2
Number of Residues1
DetailsMOD_RES: Phosphoserine; by PKA => ECO:0000269|PubMed:18202122, ECO:0007744|PubMed:19131326, ECO:0007744|PubMed:21183079
ChainResidueDetails
ASER19

site_idSWS_FT_FI3
Number of Residues1
DetailsMOD_RES: N6-succinyllysine => ECO:0007744|PubMed:23806337
ChainResidueDetails
ALYS114

227111

PDB entries from 2024-11-06

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