Structure of PDB 4rkd Chain H

Receptor sequence

>4rkdH (length=398) Species: 408968 (Psychrobacter sp. B6)

MFERIDYYAGDPILGLVEKFAADNNPDKVNLGIGIYYDESGVMPVLDCVK
IAEQRIADPISPRPYLPMAGLPGHRKGCQELLFGKDAPVLKDGLVATIAT
IGGSGALKVGAEFIHEWFPQSKCYVSDPTWGNHIAIFEGCDIEVGKYPYY
DTATGGIKFDEMIAFFETLNKDDVLLLHPCCHNPTGVDLTREQWDTVLNV
IQERELIPFMDIAYQGFGEDMDSDAYAIRKAVDMGLPLFVSNSFSKNLSL
YGERVGGLSVVCPTVDETERVFGQLNSTVRRIYSSPPSHGGRVVDIVMND
AALHEQWVGEVYAMRDRIKSMRTKLKSVLEAKISGRNFDYLTAQNGMFSF
TGLTPEQVERLQSEFGIYMISNSRMCVAGLNSSNIDYVANAMVDVLKD

3D structure

• PDB: 4rkd Crystal structure and enzymatic properties of a broad substrate-specificity psychrophilic aminotransferase from the Antarctic soil bacterium Psychrobacter sp. B6.
• Chain: H
• Resolution: 2.76 Å

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	PMP	H	G102 G103 S104 W130 D211 A213 Y214 S243 S245 K246 R254	G102 G103 S104 W130 D211 A213 Y214 S243 S245 K246 R254

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

External links

• PDB: RCSB:4rkd, PDBe:4rkd, PDBj:4rkd
• PDBsum: 4rkd
• PubMed: 25760611
• UniProt: C7E5X4