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6W80

Crystal structure of Glutamate-1-semialdehyde 2,1-aminomutase from Stenotrophomonas maltophilia K279a in complex with PLP

Functional Information from GO Data
ChainGOidnamespacecontents
A0005737cellular_componentcytoplasm
A0006779biological_processporphyrin-containing compound biosynthetic process
A0006782biological_processprotoporphyrinogen IX biosynthetic process
A0008483molecular_functiontransaminase activity
A0016853molecular_functionisomerase activity
A0030170molecular_functionpyridoxal phosphate binding
A0033014biological_processtetrapyrrole biosynthetic process
A0042286molecular_functionglutamate-1-semialdehyde 2,1-aminomutase activity
Functional Information from PDB Data
site_idAC1
Number of Residues18
Detailsbinding site for residue PLP A 500
ChainResidue
ASER116
AMET242
ALYS267
AGLY298
ATHR299
AHOH607
AHOH625
AHOH639
AHOH659
AHOH724
AGLY117
ATHR118
ATYR144
AHIS145
AGLY146
AASN211
AASP239
AVAL241

Functional Information from PROSITE/UniProt
site_idPS00600
Number of Residues37
DetailsAA_TRANSFER_CLASS_3 Aminotransferases class-III pyridoxal-phosphate attachment site. LIfDEVmt.GF.RvAlggaqahygitp....DLTtfGKiigGG
ChainResidueDetails
ALEU236-GLY272

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsMOD_RES: N6-(pyridoxal phosphate)lysine => ECO:0000255|HAMAP-Rule:MF_00375
ChainResidueDetails
ALYS267

218500

PDB entries from 2024-04-17

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