Structure of PDB 1nx9 Chain C

Receptor sequence
>1nx9C (length=617) Species: 438 (Acetobacter pasteurianus) [Search protein sequence]
HDPLSVQTGSDIPASVHMPTDQQRDYIKREVMVPMRDGVKLYTVIVIPKN
ARNAPILLTRTPYNAKGRANRVPNALTMREVLPQGDDVFVEGGYIRVFQD
IRGKYGSQGDYVMTRPPHGPLNPTKTDETTDAWDTVDWLVHNVPESNGRV
GMTGSAYEGFTVVMALLDPHPALKVAAPESPMVDGWMGDDWFHYGAFRQG
AFDYFVSQMTARGGGNDIPRRDADDYTNFLKAGSAGSFATQAGLDQYPFW
QRMHAHPAYDAFWQGQALDKILAQRKPTVPMLWEQGLWDQEDMWGAIHAW
QALKDADVKAPNTLVMGPWRHSGVNYNGSTLGPLEFEGDTAHQYRRDVFR
PFFDEYLKPGSASVHLPDAIIYNTGDQKWDYYRSWPSVCESNCTGGLTPL
YLADGHGLSFTHPAADGADSYVSDPAHPVPFISRPFAFAQSSRWKPWLVQ
DQREAESRPDVVTYETEVLDEPVRVSGVPVADLFAATSGTDSDWVVKLID
VQPAMTPDDPKMGGYELPVSMDIFRGRYRKDFAKPEALQPDATLHYHFTL
PAVNHVFAKGHRIMVQIQSSWFPLYDRNPQKFVPNIFDAKPADYTVATQS
IHHGGKEATSILLPVVK
3D structure
PDB1nx9 Acetobacter turbidans {alpha}-Amino Acid Ester Hydrolase: HOW A SINGLE MUTATION IMPROVES AN ANTIBIOTIC-PRODUCING ENZYME.
ChainC
Resolution2.2 Å
3D
structure
Catalytic site residues are labeled in the structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
Enzymatic activity
Catalytic site (original residue number in PDB) Y112 A205 Y206 Q257 D338 H370
Catalytic site (residue number reindexed from 1) Y63 A156 Y157 Q208 D289 H321
Enzyme Commision number 3.1.1.43: alpha-amino-acid esterase.
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 AIC C Y112 R117 Y154 E207 Q257 S371 Y375 Y63 R68 Y105 E158 Q208 S322 Y326
Gene Ontology
Molecular Function
GO:0008239 dipeptidyl-peptidase activity
GO:0016787 hydrolase activity
GO:0047658 alpha-amino-acid esterase activity

View graph for
Molecular Function
External links
PDB RCSB:1nx9, PDBe:1nx9, PDBj:1nx9
PDBsum1nx9
PubMed16377627
UniProtQ8VRK8

[Back to BioLiP]