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2HUU

Crystal structure of Aedes aegypti alanine glyoxylate aminotransferase in complex with alanine

Functional Information from GO Data
ChainGOidnamespacecontents
A0004760molecular_functionserine-pyruvate transaminase activity
A0005777cellular_componentperoxisome
A0008453molecular_functionalanine-glyoxylate transaminase activity
A0008483molecular_functiontransaminase activity
A0009436biological_processglyoxylate catabolic process
A0016740molecular_functiontransferase activity
A0019265biological_processglycine biosynthetic process, by transamination of glyoxylate
A0030170molecular_functionpyridoxal phosphate binding
B0004760molecular_functionserine-pyruvate transaminase activity
B0005777cellular_componentperoxisome
B0008453molecular_functionalanine-glyoxylate transaminase activity
B0008483molecular_functiontransaminase activity
B0009436biological_processglyoxylate catabolic process
B0016740molecular_functiontransferase activity
B0019265biological_processglycine biosynthetic process, by transamination of glyoxylate
B0030170molecular_functionpyridoxal phosphate binding
Functional Information from PDB Data
site_idAC1
Number of Residues7
DetailsBINDING SITE FOR RESIDUE ALA A 701
ChainResidue
APRO25
ASER155
ALLP206
ALEU347
AARG356
BHIS45
BTYR257

site_idAC2
Number of Residues7
DetailsBINDING SITE FOR RESIDUE 1BO B 801
ChainResidue
BPRO25
BSER155
BARG356
BHOH1082
BHOH1111
AHIS45
ATYR257

Functional Information from PROSITE/UniProt
site_idPS00595
Number of Residues21
DetailsAA_TRANSFER_CLASS_5 Aminotransferases class-V pyridoxal-phosphate attachment site. IDAMytGSQKvlgappGiTpV
ChainResidueDetails
AILE197-VAL217

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsBINDING: in other chain => ECO:0000269|PubMed:16990263, ECO:0007744|PDB:2HUF, ECO:0007744|PDB:2HUI, ECO:0007744|PDB:2HUU
ChainResidueDetails
ASER78
BSER78

site_idSWS_FT_FI2
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:16990263, ECO:0007744|PDB:2HUU
ChainResidueDetails
ASER155
BSER155

site_idSWS_FT_FI3
Number of Residues2
DetailsBINDING: in other chain => ECO:0000269|PubMed:16990263, ECO:0007744|PDB:2HUI, ECO:0007744|PDB:2HUU
ChainResidueDetails
AGLN205
BGLN205

site_idSWS_FT_FI4
Number of Residues4
DetailsBINDING: BINDING => ECO:0000269|PubMed:16990263, ECO:0007744|PDB:2HUI, ECO:0007744|PDB:2HUU
ChainResidueDetails
ATYR257
ATHR260
BTYR257
BTHR260

site_idSWS_FT_FI5
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:16990263, ECO:0007744|PDB:2HUI
ChainResidueDetails
AARG356
BARG356

site_idSWS_FT_FI6
Number of Residues2
DetailsMOD_RES: N6-(pyridoxal phosphate)lysine => ECO:0000255|PIRSR:PIRSR000524-50, ECO:0000269|PubMed:16990263, ECO:0007744|PDB:2HUI, ECO:0007744|PDB:2HUU
ChainResidueDetails
ALLP206
BLLP206

Catalytic Information from CSA
site_idCSA1
Number of Residues1
DetailsAnnotated By Reference To The Literature 1bjo
ChainResidueDetails
ALEU51

site_idCSA2
Number of Residues1
DetailsAnnotated By Reference To The Literature 1bjo
ChainResidueDetails
BLEU51

site_idCSA3
Number of Residues2
DetailsAnnotated By Reference To The Literature 1bjo
ChainResidueDetails
AASP180
ATRP105

site_idCSA4
Number of Residues2
DetailsAnnotated By Reference To The Literature 1bjo
ChainResidueDetails
BASP180
BTRP105

site_idCSA5
Number of Residues2
DetailsAnnotated By Reference To The Literature 1bjo
ChainResidueDetails
AHIS104
AASP180

site_idCSA6
Number of Residues2
DetailsAnnotated By Reference To The Literature 1bjo
ChainResidueDetails
BHIS104
BASP180

224931

PDB entries from 2024-09-11

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