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4RKC

Psychrophilic aromatic amino acids aminotransferase from Psychrobacter sp. B6

Functional Information from GO Data
ChainGOidnamespacecontents
A0003824molecular_functioncatalytic activity
A0004838molecular_functionL-tyrosine:2-oxoglutarate aminotransferase activity
A0005829cellular_componentcytosol
A0006520biological_processamino acid metabolic process
A0008483molecular_functiontransaminase activity
A0009058biological_processbiosynthetic process
A0030170molecular_functionpyridoxal phosphate binding
A0033585biological_processL-phenylalanine biosynthetic process from chorismate via phenylpyruvate
A0042802molecular_functionidentical protein binding
A0046872molecular_functionmetal ion binding
B0003824molecular_functioncatalytic activity
B0004838molecular_functionL-tyrosine:2-oxoglutarate aminotransferase activity
B0005829cellular_componentcytosol
B0006520biological_processamino acid metabolic process
B0008483molecular_functiontransaminase activity
B0009058biological_processbiosynthetic process
B0030170molecular_functionpyridoxal phosphate binding
B0033585biological_processL-phenylalanine biosynthetic process from chorismate via phenylpyruvate
B0042802molecular_functionidentical protein binding
B0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MG A 401
ChainResidue
AHOH770
AHOH779
AHOH780
AHOH781
AHOH782
AHOH869

site_idAC2
Number of Residues10
DetailsBINDING SITE FOR RESIDUE NO3 A 402
ChainResidue
ATRP130
AASN183
ATYR214
APHE348
AARG374
APMP409
AHOH811
AILE13
AILE33
AGLY34

site_idAC3
Number of Residues7
DetailsBINDING SITE FOR RESIDUE NO3 A 403
ChainResidue
AMET1
APHE2
AGLU3
AARG4
AILE5
AHOH540
BPHE118

site_idAC4
Number of Residues7
DetailsBINDING SITE FOR RESIDUE NO3 A 404
ChainResidue
ALEU81
AMET221
AHIS304
AVAL308
AHOH751
AHOH804
AHOH834

site_idAC5
Number of Residues5
DetailsBINDING SITE FOR RESIDUE NO3 A 405
ChainResidue
AGLU39
AARG317
AMET321
AASN381
ASER382

site_idAC6
Number of Residues6
DetailsBINDING SITE FOR RESIDUE NO3 A 406
ChainResidue
ASER277
AARG280
AARG281
AHOH853
BTYR8
BALA135

site_idAC7
Number of Residues3
DetailsBINDING SITE FOR RESIDUE NO3 A 407
ChainResidue
ATHR342
AALA343
AASN345

site_idAC8
Number of Residues3
DetailsBINDING SITE FOR RESIDUE NO3 A 408
ChainResidue
APRO72
AGLY73
ALYS76

site_idAC9
Number of Residues14
DetailsBINDING SITE FOR RESIDUE PMP A 409
ChainResidue
AGLY102
AGLY103
ASER104
ATRP130
AASN183
AASP211
ATYR214
ASER243
ASER245
ALYS246
AARG254
ANO3402
AHOH811
BTYR65

site_idBC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MG B 401
ChainResidue
AHOH526
AHOH527
BHOH542
BHOH543
BHOH544
BHOH592

site_idBC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE NO3 B 402
ChainResidue
BGLY34
BTRP130
BASN183
BARG374

site_idBC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE NO3 B 403
ChainResidue
BLEU81
BMET221
BHIS304
BHOH771

site_idBC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE NO3 B 404
ChainResidue
BLYS319
BARG322
BTHR323
BTHR342
BHOH633

site_idBC5
Number of Residues15
DetailsBINDING SITE FOR RESIDUE PMP B 405
ChainResidue
ATYR65
BGLY102
BGLY103
BSER104
BTRP130
BASN183
BASP211
BALA213
BTYR214
BSER243
BSER245
BLYS246
BARG254
BHOH591
BHOH870

Functional Information from PROSITE/UniProt
site_idPS00105
Number of Residues14
DetailsAA_TRANSFER_CLASS_1 Aminotransferases class-I pyridoxal-phosphate attachment site. SFSKnlSLyGERVG
ChainResidueDetails
ASER243-GLY256

224004

PDB entries from 2024-08-21

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