Structure of PDB 3ahm Chain B

Receptor sequence
>3ahmB (length=563) Species: 295930 (Geobacillus sp. MO-1) [Search protein sequence]
KFSEFRYERPNIEKLKASFQQALQSFQKASNAEEQNEAMKEINQLRNDFS
TMAQICYIRHTIDTNDEFYKQEQDFFDEVEPIVKGLVNDYYRALVSSPFR
SQLEGKWGKQLFALAEAELKTYSPDIVEDLQLENKLTSEYTKLVASAKIF
FEGEERTLAQLQPFVESPDRDMRKRASEARFTFFQEHEEKFDEIYDQLVK
VRTAIAQKLGFKNFVELGYARLGRTDYNAEMVAKFRKQVEKHIVPIAVKL
RERQRERIGVEKLKYYDEAFVFPTGNPMPKGDANWIIENGKKMYEELSPE
TGEFFRYMIEHELMDLVAKKGKASGGYCTYIENYKAPFIFSNFTGTSGDI
DVLTHEAGHAFQVYESRHYEIPEYNWPTLEACEIHSMSMEFFTWPWMKLF
FKEDAEKYQFYHLSDALLFLPYGVAVDEFQHFVYENPNATPAERKQAWRA
IERKYMPTKDYDGNDYLERGGFWQRQSHIYTTAFYYIDYTLAQICAFQFW
KRSRENYKEAWNDYLTLCRQGGSKPFTELVRVANLISPFEDGCVQSVVGG
IEGWLNSVDDQSL
3D structure
PDB3ahm The exquisite structure and reaction mechanism of bacterial Pz-peptidase A toward collagenous peptides: X-ray crystallographic structure analysis of PZ-peptidase a reveals differences from mammalian thimet oligopeptidase.
ChainB
Resolution2.0 Å
3D
structure
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Enzymatic activity
Enzyme Commision number ?
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 H356 H360 E384 H355 H359 E383
Gene Ontology
Molecular Function
GO:0004222 metalloendopeptidase activity
GO:0046872 metal ion binding
Biological Process
GO:0006508 proteolysis
GO:0006518 peptide metabolic process

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Molecular Function
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Biological Process
External links
PDB RCSB:3ahm, PDBe:3ahm, PDBj:3ahm
PDBsum3ahm
PubMed20817732
UniProtQ4W803

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