Structure of PDB 3aho Chain A

Receptor sequence
>3ahoA (length=564) Species: 295930 (Geobacillus sp. MO-1) [Search protein sequence]
MKFSEFRYERPNIEKLKASFQQALQSFQKASNAEEQNEAMKEINQLRNDF
STMAQICYIRHTIDTNDEFYKQEQDFFDEVEPIVKGLVNDYYRALVSSPF
RSQLEGKWGKQLFALAEAELKTYSPDIVEDLQLENKLTSEYTKLVASAKI
FFEGEERTLAQLQPFVESPDRDMRKRASEARFTFFQEHEEKFDEIYDQLV
KVRTAIAQKLGFKNFVELGYARLGRTDYNAEMVAKFRKQVEKHIVPIAVK
LRERQRERIGVEKLKYYDEAFVFPTGNPMPKGDANWIIENGKKMYEELSP
ETGEFFRYMIEHELMDLVAKKGKASGGYCTYIENYKAPFIFSNFTGTSGD
IDVLTHEAGHAFQVYESRHYEIPEYNWPTLEACEIHSMSMEFFTWPWMKL
FFKEDAEKYQFYHLSDALLFLPYGVAVDEFQHFVYENPNATPAERKQAWR
AIERKYMPTKDYDGNDYLERGGFWQRQSHIYTTAFYYIDYTLAQICAFQF
WKRSRENYKEAWNDYLTLCRQGGSKPFTELVRVANLISPFEDGCVQSVVG
GIEGWLNSVDDQSL
3D structure
PDB3aho 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.
ChainA
Resolution1.88 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 A H356 H360 E384 H356 H360 E384
BS02 3A2 A G327 Y328 C329 H356 E357 H360 W377 L380 E384 R476 Q477 H479 Y486 Y487 Y490 G327 Y328 C329 H356 E357 H360 W377 L380 E384 R476 Q477 H479 Y486 Y487 Y490 MOAD: Ki=88.9nM
PDBbind-CN: -logKd/Ki=7.05,Ki=88.9nM
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:3aho, PDBe:3aho, PDBj:3aho
PDBsum3aho
PubMed20817732
UniProtQ4W803

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