Structure of PDB 4ger Chain A

Receptor sequence
>4gerA (length=304) Species: 1406 (Paenibacillus polymyxa) [Search protein sequence]
ATGTGKGVLGDTKSFTTTASGSSYQLKDTTRGNGVVTYTASNRQSIPGTI
LTDADNVWNDPAGVDAHTYAAKTYDYYKAKFGRNSIDGRGLQLRSTVHYG
SRYNNAFWNGSQMTYGDGDGSTFIAFSGDPDVVGHELTHGVTEYTSNLEY
YGESGALNEAFSDVIGNDIQRKNWLVGDDIYTPNIAGDALRSMSNPTLYD
QPDHYSNLYTGSSDNGGVHTNSGIINKAYYLLAQGGTFHGVTVNGIGRDA
AVQIYYSAFTNYLTSSSDFSNARAAVIQAAKDQYGANSAEATAAAKSFDA
VGVN
3D structure
PDB4ger Structure of Gentlyase, the neutral metalloprotease of Paenibacillus polymyxa.
ChainA
Resolution1.59 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) H135 E136 H139 Y150 E159 D214 H219
Catalytic site (residue number reindexed from 1) H135 E136 H139 Y150 E159 D214 H219
Enzyme Commision number 3.4.24.28: bacillolysin.
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 H135 H139 E159 H135 H139 E159
BS02 CA A D129 D131 Q170 D178 D179 D129 D131 Q170 D178 D179
BS03 CA A D53 D55 V57 D53 D55 V57
BS04 CA A Y181 T182 I185 D188 Y181 T182 I185 D188
BS05 THR A E136 R191 E136 R191
BS06 LYS A N104 N105 F123 H219 N104 N105 F123 H219
Gene Ontology
Molecular Function
GO:0004222 metalloendopeptidase activity
Biological Process
GO:0006508 proteolysis

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Molecular Function
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Biological Process
External links
PDB RCSB:4ger, PDBe:4ger, PDBj:4ger
PDBsum4ger
PubMed23275160
UniProtP29148|NPRE_PAEPO Bacillolysin (Gene Name=npr)

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