Structure of PDB 6cek Chain A

Receptor sequence

>6cekA (length=713) Species: 320372 (Burkholderia pseudomallei 1710b)

GTSNRDWWPNQLDLSILHRHSSLSDPMGKDFNYAQAFEKLDLAAVKRDLH
ALMTTSQDWWPADFGHYGGLFIRMAWHSAGTYRTADGRGGAGEGQQRFAP
LNSWPNNANLDKARRLLWPIKQKYGRAISWADLLILTGNVALESMGFKTF
GFAGGRADTWEPEDVYWGSEKIWLELSGGPNSRYSGDRQLENPLAAVQMG
LIYVNPEGPDGNPDPVAAARDIRDTFARMAMNDEETVALIAGGHTFGKTH
GAGPASNVGAEPEAAGIEAQGLGWKSAYRTGKGADAITSGLEVTWTTTPT
QWSHNFFENLFGYEWELTKSPAGAHQWVAKGADAVIPDAFDPSKKHRPTM
LTTDLSLRFDPAYEKISRRFHENPEQFADAFARAWFKLTHRDMGPRARYL
GPEVPAEVLLWQDPIPAVDHPLIDAADAAELKAKVLASGLTVSQLVSTAW
AAASTFRGSDKRGGANGARIRLAPQKDWEANQPEQLAAVLETLEAIRTAF
NGAQRGGKQVSLADLIVLAGCAGVEQAAKNAGHAVTVPFAPGRADASQEQ
TDVESMAVLEPVADGFRNYLKGKYRVPAEVLLVDKAQLLTLSAPEMTVLL
GGLRVLGANVGQSRHGVFTAREQALTNDFFVNLLDMGTEWKPTAADADVF
EGRDRATGELKWTGTRVDLVFGSHSQLRALAEVYGSADAQEKFVRDFVAV
WNKVMNLDRFDLA

3D structure

• PDB: 6cek Crystal structure of the D141N variant of catalase-peroxidase from B. pseudomallei
• Chain: A
• Resolution: 1.8 Å

Enzymatic activity

• Enzyme Commision number: 1.11.1.21: catalase peroxidase.

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	HEM	A	G104 L105 I107 R108 X111 V239 P241 L274 I275 G278 H279 K283 T284 H285 T323 S324 W330 W420	G69 L70 I72 R73 X76 V204 P206 L239 I240 G243 H244 K248 T249 H250 T288 S289 W295 W385
BS02	OXY	A	R108 H112 N141	R73 H77 N106

Gene Ontology

Molecular Function

• GO:0004096 catalase activity
• GO:0004601 peroxidase activity
• GO:0020037 heme binding
• GO:0046872 metal ion binding

Biological Process

• GO:0006979 response to oxidative stress
• GO:0042744 hydrogen peroxide catabolic process
• GO:0070301 cellular response to hydrogen peroxide
• GO:0098869 cellular oxidant detoxification

Cellular Component

• GO:0005829 cytosol

External links

• PDB: RCSB:6cek, PDBe:6cek, PDBj:6cek
• PDBsum: 6cek
• UniProt: Q3JNW6|KATG_BURP1 Catalase-peroxidase (Gene Name=katG)