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4PPM

Crystal structure of PigE: a transaminase involved in the biosynthesis of 2-methyl-3-n-amyl-pyrrole (MAP) from Serratia sp. FS14

Functional Information from GO Data
ChainGOidnamespacecontents
A0008483molecular_functiontransaminase activity
A0017000biological_processantibiotic biosynthetic process
A0030170molecular_functionpyridoxal phosphate binding
A0042802molecular_functionidentical protein binding
A0070280molecular_functionpyridoxal binding
B0008483molecular_functiontransaminase activity
B0017000biological_processantibiotic biosynthetic process
B0030170molecular_functionpyridoxal phosphate binding
B0042802molecular_functionidentical protein binding
B0070280molecular_functionpyridoxal binding
Functional Information from PDB Data
site_idAC1
Number of Residues3
DetailsBINDING SITE FOR RESIDUE MG A 901
ChainResidue
AALA722
ATYR725
AVAL728

site_idAC2
Number of Residues14
DetailsBINDING SITE FOR RESIDUE PLP A 902
ChainResidue
AVAL618
AGLN619
ALYS645
AHOH1007
AHOH1054
AHOH1055
BTHR680
BHOH1026
AGLY503
ATHR504
ATYR530
AHIS531
AGLU583
AASP616

site_idAC3
Number of Residues3
DetailsBINDING SITE FOR RESIDUE MG B 901
ChainResidue
BALA722
BTYR725
BVAL728

site_idAC4
Number of Residues15
DetailsBINDING SITE FOR RESIDUE PLP B 902
ChainResidue
ATHR680
AHOH1017
BSER502
BGLY503
BTHR504
BTYR530
BHIS531
BGLU588
BASP616
BVAL618
BGLN619
BLYS645
BHOH1049
BHOH1050
BHOH1051

Functional Information from PROSITE/UniProt
site_idPS00600
Number of Residues38
DetailsAA_TRANSFER_CLASS_3 Aminotransferases class-III pyridoxal-phosphate attachment site. LMvDEVqt.GLgRtGklfacewdgiep....DVLmlSKslsGG
ChainResidueDetails
ALEU613-GLY650

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsBINDING: BINDING => ECO:0000269|PubMed:24704447
ChainResidueDetails
AGLY503
ATHR680
BGLY503
BTHR680

site_idSWS_FT_FI2
Number of Residues2
DetailsMOD_RES: N6-(pyridoxal phosphate)lysine => ECO:0000269|PubMed:24704447
ChainResidueDetails
ALYS645
BLYS645

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PDB entries from 2024-08-21

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