Structure of PDB 1qhb Chain C

Receptor sequence
>1qhbC (length=595) Species: 35170 (Corallina officinalis) [Search protein sequence]
GIPADNLQSRAKASFDTRVAAAELALARGAVPSFANGEELLYRNSETGDP
SFIGSFTKGLPHDDNGAIIDPDDFLAFVRAINSGDEKEIAALTLGPARDP
ETGLPIWRSDLANSLDLEVRGWENSSAGLTFDLEGPDAQSVAMPPAPVLT
SPELIAEMAELYLMALGRDIEFSEFDSPKNAAFIRSAIERLNGLEWFNTP
AKLGDPPAEIRRRRGEVTVGNLFRGILPGSEVGPYLSQFIIVGSKQIGSA
TVGNKTLVSPNAADEFDGEIAYGSITISQRVRIATPGRDFMTDLKVFLDV
QDAADFRGFESYEPGARLIRTIRDLATWVHFDSLYEAYLNACLILLANGV
PFDPNLPFQQEDKLDNQDVFVNFGSAHVLSLVTEVATRALKAVRYQKFNI
HRRLRPEATGGLISVNKNAFLKSESVFPEVDVLVEELSSILDDSASSNEK
QNIADGDVSPGKSFLLPMAFAEGSPFHPSYGSGHAVVAGACVTILKAFFD
ANFQIDQVFEVDTDEDKLVKSSFPGPLTVAGELNKLADNVAIGRNMAGVH
YFSDQFESLLLGEQIAIGILEEQSLTYGENFFFNLPKFDGTTIQI
3D structure
PDB1qhb Crystal structure of dodecameric vanadium-dependent bromoperoxidase from the red algae Corallina officinalis.
ChainC
Resolution2.3 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) K398 R406 H478 S483 G484 H485 R545 H551 D555
Catalytic site (residue number reindexed from 1) K397 R405 H477 S482 G483 H484 R544 H550 D554
Enzyme Commision number 1.11.1.18: bromide 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 CA C F359 Q361 D363 D366 Q368 F358 Q360 D362 D365 Q367
Gene Ontology
Molecular Function
GO:0004601 peroxidase activity
GO:0019806 bromide peroxidase activity
GO:0046872 metal ion binding
Biological Process
GO:0098869 cellular oxidant detoxification

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Molecular Function
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Biological Process
External links
PDB RCSB:1qhb, PDBe:1qhb, PDBj:1qhb
PDBsum1qhb
PubMed10843856
UniProtQ8LLW7|PRXV_COROI Vanadium-dependent bromoperoxidase

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