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3DOD

Crystal Structure of PLP Bound 7,8-Diaminopelargonic Acid Synthase in Bacillus subtilis

Functional Information from GO Data
ChainGOidnamespacecontents
A0003824molecular_functioncatalytic activity
A0004015molecular_functionadenosylmethionine-8-amino-7-oxononanoate transaminase activity
A0005737cellular_componentcytoplasm
A0008483molecular_functiontransaminase activity
A0009102biological_processbiotin biosynthetic process
A0030170molecular_functionpyridoxal phosphate binding
B0003824molecular_functioncatalytic activity
B0004015molecular_functionadenosylmethionine-8-amino-7-oxononanoate transaminase activity
B0005737cellular_componentcytoplasm
B0008483molecular_functiontransaminase activity
B0009102biological_processbiotin biosynthetic process
B0030170molecular_functionpyridoxal phosphate binding
Functional Information from PDB Data
site_idAC1
Number of Residues10
DetailsBINDING SITE FOR RESIDUE PLP A 501
ChainResidue
ATRP54
BSER317
ASER112
AGLY113
AALA114
AGLU217
AASP251
AALA254
ALYS280
BHIS316

site_idAC2
Number of Residues10
DetailsBINDING SITE FOR RESIDUE PLP B 502
ChainResidue
AHIS316
ASER317
BTRP54
BSER112
BGLY113
BALA114
BGLU217
BASP251
BALA254
BLYS280

Functional Information from PROSITE/UniProt
site_idPS00600
Number of Residues38
DetailsAA_TRANSFER_CLASS_3 Aminotransferases class-III pyridoxal-phosphate attachment site. MIvDEVat.GFgRtGkmfacehenvqp....DLMaaGKgitGG
ChainResidueDetails
AMET248-GLY285

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsBINDING: BINDING => ECO:0000269|PubMed:20565114, ECO:0007744|PDB:3DOD, ECO:0007744|PDB:3DU4
ChainResidueDetails
AGLY113
AHIS316
BGLY113
BHIS316

site_idSWS_FT_FI2
Number of Residues6
DetailsBINDING: BINDING => ECO:0000269|PubMed:20565114, ECO:0007744|PDB:3DU4
ChainResidueDetails
ATYR146
AGLY315
AARG410
BTYR146
BGLY315
BARG410

site_idSWS_FT_FI3
Number of Residues2
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:P12995
ChainResidueDetails
AASP251
BASP251

site_idSWS_FT_FI4
Number of Residues2
DetailsMOD_RES: N6-(pyridoxal phosphate)lysine => ECO:0000269|PubMed:20565114, ECO:0007744|PDB:3DOD, ECO:0007744|PDB:3DU4
ChainResidueDetails
ALYS280
BLYS280

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1b8g
ChainResidueDetails
ALYS280
AASP251

site_idCSA2
Number of Residues2
DetailsAnnotated By Reference To The Literature 1b8g
ChainResidueDetails
BLYS280
BASP251

site_idCSA3
Number of Residues1
DetailsAnnotated By Reference To The Literature 1b8g
ChainResidueDetails
AASP111

site_idCSA4
Number of Residues1
DetailsAnnotated By Reference To The Literature 1b8g
ChainResidueDetails
BASP111

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PDB entries from 2024-10-02

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