Structure of PDB 3k5x Chain A

Receptor sequence
>3k5xA (length=391) Species: 1902 (Streptomyces coelicolor) [Search protein sequence]
MTSLEKARELLREFPVVDGHNDLPWALREQVRYDLDARDIAADQSAHLHT
DLARLRSGGVGAQYWSVYVRSDLPGAVTATLEQIDCVRRLIDRHPGELRA
ALTAADMEAARAEGRIASLMGAEGGHSIDNSLATLRALYALGVRYMTLTH
NDNNAWADSATDEPGVGGLSAFGREVVREMNREGMLVDLSHVAATTMRDA
LDTSTAPVIFSHSSSRAVCDHPRNIPDDVLERLSANGGMAMVTFVPKFVL
QAAVDWTAEADDNMRAHGFHHLDSSPEAMKVHAAFEERVPRPVATVSTVA
DHLDHMREVAGVDHLGIGGDYDGTPFTPDGLGDVSGYPNLIAELLDRGWS
QSDLAKLTWKNAVRVLDAAEDVSRGLRAARGPSNATIEQLD
3D structure
PDB3k5x Structure, mechanism, and substrate profile for Sco3058: the closest bacterial homologue to human renal dipeptidase .
ChainA
Resolution1.4 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) H20 D22 E123 H150 H191 H212 D320
Catalytic site (residue number reindexed from 1) H20 D22 E123 H150 H191 H212 D320
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 P8D A H20 D22 Y68 E123 H150 H191 H212 R223 F248 D320 G323 T324 H20 D22 Y68 E123 H150 H191 H212 R223 F248 D320 G323 T324 MOAD: Ki=390nM
PDBbind-CN: -logKd/Ki=6.41,Ki=390nM
BS02 ZN A H20 D22 E123 H20 D22 E123
BS03 ZN A E123 H191 H212 E123 H191 H212
Gene Ontology
Molecular Function
GO:0046872 metal ion binding
GO:0070573 metallodipeptidase activity
Biological Process
GO:0006508 proteolysis

View graph for
Molecular Function

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Biological Process
External links
PDB RCSB:3k5x, PDBe:3k5x, PDBj:3k5x
PDBsum3k5x
PubMed20000809
UniProtQ93J45

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