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2ZSL

Crystal structure of glutamate-1-semialdehyde 2,1-aminomutase from Aeropyrum pernix

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 Residues19
DetailsBINDING SITE FOR RESIDUE PMP A 501
ChainResidue
ASER120
AVAL246
ALYS271
AGLY302
ATHR303
APHE304
AHOH520
AHOH551
AHOH602
AHOH714
AHOH749
AGLY121
ATHR122
ATYR148
AHIS149
AGLU210
AASN215
AASP243
AVAL245

Functional Information from PROSITE/UniProt
site_idPS00600
Number of Residues37
DetailsAA_TRANSFER_CLASS_3 Aminotransferases class-III pyridoxal-phosphate attachment site. LIlDEVvt.GF.RlGlegaqgyfnieg....DIIvlGKiigGG
ChainResidueDetails
ALEU240-GLY276

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsMOD_RES: N6-(pyridoxal phosphate)lysine => ECO:0000250
ChainResidueDetails
ALYS271

Catalytic Information from CSA
site_idCSA1
Number of Residues3
DetailsAnnotated By Reference To The Literature 1ay4
ChainResidueDetails
AASP243
ATYR148
ALYS271

site_idCSA2
Number of Residues1
DetailsAnnotated By Reference To The Literature 1ay4
ChainResidueDetails
AASP243

227111

PDB entries from 2024-11-06

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