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2III

Crystal structure of the adenosylmethionine decarboxylase (aq_254) from aquifex aeolicus vf5

Functional Information from GO Data
ChainGOidnamespacecontents
A0004014molecular_functionadenosylmethionine decarboxylase activity
A0005829cellular_componentcytosol
A0008295biological_processspermidine biosynthetic process
A0016831molecular_functioncarboxy-lyase activity
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MG A 136
ChainResidue
AASP19
AASP22
AASP26
AHOH181
AHOH226

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CA A 137
ChainResidue
AGLU32
ALYS42
ASER45
ATYR47

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Schiff-base intermediate with substrate; via pyruvic acid => ECO:0000255|HAMAP-Rule:MF_00464
ChainResidueDetails
ASER64

site_idSWS_FT_FI2
Number of Residues1
DetailsACT_SITE: Proton acceptor; for processing activity => ECO:0000255|HAMAP-Rule:MF_00464
ChainResidueDetails
AHIS69

site_idSWS_FT_FI3
Number of Residues1
DetailsACT_SITE: Proton donor; for catalytic activity => ECO:0000255|HAMAP-Rule:MF_00464
ChainResidueDetails
ACYS84

site_idSWS_FT_FI4
Number of Residues1
DetailsSITE: Cleavage (non-hydrolytic); by autolysis => ECO:0000255|HAMAP-Rule:MF_00464
ChainResidueDetails
AGLU63

site_idSWS_FT_FI5
Number of Residues1
DetailsMOD_RES: Pyruvic acid (Ser); by autocatalysis => ECO:0000255|HAMAP-Rule:MF_00464
ChainResidueDetails
ASER64

224201

PDB entries from 2024-08-28

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