Structure of PDB 4rkd Chain G

Receptor sequence
>4rkdG (length=398) Species: 408968 (Psychrobacter sp. B6) [Search protein sequence]
MFERIDYYAGDPILGLVEKFAADNNPDKVNLGIGIYYDESGVMPVLDCVK
IAEQRIADPISPRPYLPMAGLPGHRKGCQELLFGKDAPVLKDGLVATIAT
IGGSGALKVGAEFIHEWFPQSKCYVSDPTWGNHIAIFEGCDIEVGKYPYY
DTATGGIKFDEMIAFFETLNKDDVLLLHPCCHNPTGVDLTREQWDTVLNV
IQERELIPFMDIAYQGFGEDMDSDAYAIRKAVDMGLPLFVSNSFSKNLSL
YGERVGGLSVVCPTVDETERVFGQLNSTVRRIYSSPPSHGGRVVDIVMND
AALHEQWVGEVYAMRDRIKSMRTKLKSVLEAKISGRNFDYLTAQNGMFSF
TGLTPEQVERLQSEFGIYMISNSRMCVAGLNSSNIDYVANAMVDVLKD
3D structure
PDB4rkd Crystal structure and enzymatic properties of a broad substrate-specificity psychrophilic aminotransferase from the Antarctic soil bacterium Psychrobacter sp. B6.
ChainG
Resolution2.76 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) W130 D211 A213 K246
Catalytic site (residue number reindexed from 1) W130 D211 A213 K246
Enzyme Commision number 2.6.1.-
Interaction with ligand
Site
#
Ligand Ligand
chain
Binding residues on receptor
(original residue number in PDB)
Binding residues on receptor
(residue number reindexed from 1)
Binding affinity
BS01 KET G G102 G103 S104 W130 N183 D211 A213 Y214 S243 S245 K246 R254 R374 G102 G103 S104 W130 N183 D211 A213 Y214 S243 S245 K246 R254 R374
Gene Ontology
Molecular Function
GO:0003824 catalytic activity
GO:0004838 L-tyrosine-2-oxoglutarate transaminase activity
GO:0008483 transaminase activity
GO:0030170 pyridoxal phosphate binding
GO:0042802 identical protein binding
GO:0046872 metal ion binding
Biological Process
GO:0006520 amino acid metabolic process
GO:0009058 biosynthetic process
GO:0033585 L-phenylalanine biosynthetic process from chorismate via phenylpyruvate
Cellular Component
GO:0005829 cytosol

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Molecular Function

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Biological Process

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Cellular Component
External links
PDB RCSB:4rkd, PDBe:4rkd, PDBj:4rkd
PDBsum4rkd
PubMed25760611
UniProtC7E5X4

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