Structure of PDB 1h8l Chain A

Receptor sequence
>1h8lA (length=380) [Search protein sequence]
QAVQPVDFRHHHFSDMEIFLRRYANEYPSITRLYSVGKSVELRELYVMEI
SDNPGIHEAGEPEFKYIGNMHGNEVVGRELLLNLIEYLCKNFGTDPEVTD
LVQSTRIHIMPSMNPDGYEKSQEGDRGGTVGRNNSNNYDLNRNFPDQFFQ
VTDPPQPETLAVMSWLKTYPFVLSANLHGGSLVVNYPFDDDEQGIAIYSK
SPDDAVFQQLALSYSKENKKMYQGSPCKDLYPTEYFPHGITNGAQWYNVP
GGMQDWNYLNTNCFEVTIELGCVKYPKAEELPKYWEQNRRSLLQFIKQVH
RGIWGFVLDATDGRGILNATISVADINHPVTTYKDGDYWRLLVQGTYKVT
ASARGYDPVTKTVEVDSKGGVQVNFTLSRT
3D structure
PDB1h8l The crystal structure of the inhibitor-complexed carboxypeptidase D domain II and the modeling of regulatory carboxypeptidases.
ChainA
Resolution2.6 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 3.4.17.22: metallocarboxypeptidase D.
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 GEM A H74 E77 R135 N144 R145 H181 N188 D192 G246 Y250 V252 E272 H71 E74 R132 N141 R142 H178 N185 D189 G243 Y247 V249 E269 PDBbind-CN: -logKd/Ki=7.47,Ki=34nM
BS02 ZN A H74 E77 H181 H71 E74 H178
Gene Ontology
Molecular Function
GO:0004180 carboxypeptidase activity
GO:0004181 metallocarboxypeptidase activity
GO:0008237 metallopeptidase activity
GO:0008270 zinc ion binding
GO:0046872 metal ion binding
Biological Process
GO:0006508 proteolysis
GO:0006518 peptide metabolic process
GO:0016485 protein processing
Cellular Component
GO:0005615 extracellular space
GO:0016020 membrane

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:1h8l, PDBe:1h8l, PDBj:1h8l
PDBsum1h8l
PubMed11278909
UniProtP83852|CBPD_LOPSP Carboxypeptidase D (Fragment) (Gene Name=CPD)

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