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

2B4D

SSAT+COA+SP- SP disordered

Functional Information from GO Data
ChainGOidnamespacecontents
A0001525biological_processangiogenesis
A0004145molecular_functiondiamine N-acetyltransferase activity
A0005515molecular_functionprotein binding
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0006596biological_processpolyamine biosynthetic process
A0008080molecular_functionN-acetyltransferase activity
A0009447biological_processputrescine catabolic process
A0016740molecular_functiontransferase activity
A0016746molecular_functionacyltransferase activity
A0016747molecular_functionacyltransferase activity, transferring groups other than amino-acyl groups
A0019809molecular_functionspermidine binding
A0032918biological_processspermidine acetylation
A0042127biological_processregulation of cell population proliferation
A0042802molecular_functionidentical protein binding
B0001525biological_processangiogenesis
B0004145molecular_functiondiamine N-acetyltransferase activity
B0005515molecular_functionprotein binding
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0006596biological_processpolyamine biosynthetic process
B0008080molecular_functionN-acetyltransferase activity
B0009447biological_processputrescine catabolic process
B0016740molecular_functiontransferase activity
B0016746molecular_functionacyltransferase activity
B0016747molecular_functionacyltransferase activity, transferring groups other than amino-acyl groups
B0019809molecular_functionspermidine binding
B0032918biological_processspermidine acetylation
B0042127biological_processregulation of cell population proliferation
B0042802molecular_functionidentical protein binding
Functional Information from PDB Data
site_idAC1
Number of Residues12
DetailsBINDING SITE FOR RESIDUE COA B 200
ChainResidue
BGLU62
BPHE139
BARG142
BARG143
BVAL96
BARG101
BGLY102
BPHE103
BGLY104
BILE105
BGLY106
BSER107

site_idAC2
Number of Residues10
DetailsBINDING SITE FOR RESIDUE COA A 201
ChainResidue
AARG101
AGLY102
APHE103
AGLY104
AGLY106
ASER107
APHE139
AARG142
AARG143
AHOH231

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Proton donor => ECO:0000250|UniProtKB:P0A951
ChainResidueDetails
BTYR140

site_idSWS_FT_FI2
Number of Residues8
DetailsBINDING: BINDING => ECO:0000305|PubMed:17516632
ChainResidueDetails
BTYR27
BGLU92
BPHE94
BGLY102
BHIS126
BASN133
BTYR140
BGLU152

235183

PDB entries from 2025-04-23

PDB statisticsPDBj update infoContact PDBjnumon