Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

6PK1

Alanine-glyoxylate aminotransferase 1 (AGT1) from Arabidopsis thaliana in presence of serine

Functional Information from GO Data
ChainGOidnamespacecontents
A0003729molecular_functionmRNA binding
A0004760molecular_functionserine-pyruvate transaminase activity
A0005739cellular_componentmitochondrion
A0005777cellular_componentperoxisome
A0005829cellular_componentcytosol
A0005886cellular_componentplasma membrane
A0008453molecular_functionalanine-glyoxylate transaminase activity
A0008483molecular_functiontransaminase activity
A0009507cellular_componentchloroplast
A0009570cellular_componentchloroplast stroma
A0009853biological_processphotorespiration
A0048046cellular_componentapoplast
A0050281molecular_functionserine-glyoxylate transaminase activity
B0003729molecular_functionmRNA binding
B0004760molecular_functionserine-pyruvate transaminase activity
B0005739cellular_componentmitochondrion
B0005777cellular_componentperoxisome
B0005829cellular_componentcytosol
B0005886cellular_componentplasma membrane
B0008453molecular_functionalanine-glyoxylate transaminase activity
B0008483molecular_functiontransaminase activity
B0009507cellular_componentchloroplast
B0009570cellular_componentchloroplast stroma
B0009853biological_processphotorespiration
B0048046cellular_componentapoplast
B0050281molecular_functionserine-glyoxylate transaminase activity
Functional Information from PDB Data
site_idAC1
Number of Residues16
Detailsbinding site for residue PLP A 501
ChainResidue
ATHR68
AGLN200
ALYS201
ATYR249
ATHR250
A3PY502
AHOH606
AHOH660
AGLY69
ATHR70
ATRP73
APHE95
AASN146
ATHR148
AASP175
AVAL177

site_idAC2
Number of Residues12
Detailsbinding site for residue 3PY A 502
ChainResidue
APRO15
AGLY16
ATYR35
AARG36
APHE95
ATHR148
ALYS201
ATHR250
AARG347
APLP501
AHOH606
AHOH701

site_idAC3
Number of Residues15
Detailsbinding site for residue PLP B 501
ChainResidue
BTHR68
BGLY69
BTHR70
BTRP73
BPHE95
BASN146
BTHR148
BASP175
BVAL177
BGLN200
BLYS201
BTYR249
BTHR250
BHOH630
BHOH667

Functional Information from PROSITE/UniProt
site_idPS00595
Number of Residues21
DetailsAA_TRANSFER_CLASS_5 Aminotransferases class-V pyridoxal-phosphate attachment site. VDVAltGSQKalslptGlGiV
ChainResidueDetails
AVAL192-VAL212

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues6
DetailsBINDING: BINDING => ECO:0000269|PubMed:31681359, ECO:0007744|PDB:6PK1, ECO:0007744|PDB:6PK3
ChainResidueDetails
ATHR68
ATHR148
AGLN200
BTHR68
BTHR148
BGLN200

site_idSWS_FT_FI2
Number of Residues4
DetailsBINDING: BINDING => ECO:0000269|PubMed:31681359, ECO:0007744|PDB:6PK1
ChainResidueDetails
ALYS201
AARG347
BLYS201
BARG347

site_idSWS_FT_FI3
Number of Residues2
DetailsMOD_RES: N-acetylmethionine => ECO:0007744|PubMed:22223895
ChainResidueDetails
AMET1
BMET1

site_idSWS_FT_FI4
Number of Residues2
DetailsMOD_RES: N6-(pyridoxal phosphate)lysine => ECO:0000250
ChainResidueDetails
ALYS201
BLYS201

site_idSWS_FT_FI5
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:22092075
ChainResidueDetails
ASER204
BSER204

221371

PDB entries from 2024-06-19

PDB statisticsPDBj update infoContact PDBjnumon