Structure of PDB 3mf3 Chain E

Receptor sequence
>3mf3E (length=215) Species: 727 (Haemophilus influenzae) [Search protein sequence]
DKIKQLFANNYSWAQRMKEENSTYFKELADHQTPHYLWIGCSDSRVPAEK
LTNLEPGELFVHRNVANQVIHTDFNCLSVVQYAVDVLKIEHIIICGHTNC
GGIHAAMADKDLGLINNWLLHIRDIWFKHGHLLGKLSPEKRADMLTKINV
AEQVYNLGRTSIVKSAWERGQKLSLHGWVYDVNDGFLVDQGVMATSRETL
EISYRNAIARLSILD
3D structure
PDB3mf3 The Structure and Properties of Cobalt(II)-Substituted Haemophilus influenzae B-Carbonic Anhydrase.
ChainE
Resolution2.5 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) C42 D44 R46 H98 C101
Catalytic site (residue number reindexed from 1) C41 D43 R45 H97 C100
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 CO E C42 D44 H98 C101 C41 D43 H97 C100
Gene Ontology
Molecular Function
GO:0004089 carbonate dehydratase activity
GO:0008270 zinc ion binding
GO:0016829 lyase activity
GO:0046872 metal ion binding
Biological Process
GO:0015976 carbon utilization
Cellular Component
GO:0005575 cellular_component

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:3mf3, PDBe:3mf3, PDBj:3mf3
PDBsum3mf3
PubMed
UniProtP45148|CAN_HAEIN Carbonic anhydrase 2 (Gene Name=can)

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