Structure of PDB 1ddz Chain B

Receptor sequence
>1ddzB (length=481) Species: 35688 (Porphyridium purpureum) [Search protein sequence]
VMSDLEKKFIELEAKLVAQPAGQAMPGKSNIFANNEAWRQEMLKQDPEFF
NRLANGQSPEYLWIGCADSRVPANQLLDLPAGEVFVHRNIANQCIHSDIS
FLSVLQYAVQYLKVKHILVCGHYGCGGAKAALGDSRLGLIDNWLRHIRDV
RRMNAKYLDKCKDGDEELNRLIELNVLEQVHNVCATSIVQDAWDAGQELT
VQGVVYGVGDGKLRDLGVVVNSSDDISKFYRTKSDSGALKAGNPNAPLVQ
VTKGGESELDSTMEKLTAELVQQTPGKLKEGANRVFVNNENWRQKMLKQD
PQFFSNLAHTQTPEILWIGCADSRVPANQIINLPAGEVFVHRNIANQCIH
SDMSFLSVLQYAVQYLKVKRVVVCGHYACGGCAAALGDSRLGLIDNWLRH
IRDVRRHNQAELSRITDPKDSLNRLIEINVLEQMHNVCATSIVQDAWDAG
QELEVQGVVYGVGDGKLRDMGVVAKANDDIG
3D structure
PDB1ddz X-ray structure of beta-carbonic anhydrase from the red alga, Porphyridium purpureum, reveals a novel catalytic site for CO(2) hydration.
ChainB
Resolution2.2 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) C149 D151 R153 H205 C208
Catalytic site (residue number reindexed from 1) C66 D68 R70 H122 C125
Enzyme Commision number 4.2.1.1: carbonic anhydrase.
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 ZN B C149 D151 H205 C208 C66 D68 H122 C125
BS02 ZN B C403 D405 H459 C462 C320 D322 H376 C379
Gene Ontology
Molecular Function
GO:0004089 carbonate dehydratase activity
GO:0008270 zinc ion binding
Biological Process
GO:0015976 carbon utilization

View graph for
Molecular Function
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Biological Process
External links
PDB RCSB:1ddz, PDBe:1ddz, PDBj:1ddz
PDBsum1ddz
PubMed10681531
UniProtQ43060

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