Structure of PDB 4d9m Chain B

Receptor sequence
>4d9mB (length=383) Species: 83333 (Escherichia coli K-12) [Search protein sequence]
SVFSLKIDIADNKFFNGETSPLFSQSQAKLARQFHQKIAGYRPTPLCALD
DLANLFGVKKILVKDESKRFGLNAFKMLGGAYAIAQLLCEKYHLDIETLS
FEEKMTFATTTDGNHGRGVAWAAQQLGQNAVIYMPKGSAQERVDAILNLG
AECIVTDMNYDDTVRLTMQHAQQHGWEVVQDTAWEGYTKIPTWIMQGYAT
LADEAVEQMREMGVTPTHVLLQAGVGAMAGGVLGYLVDVYSPQNLHSIIV
EPDKADCIYRSGVKGDIVATIMAGLACGEPNPLGWEILRNCATQFISCQD
SVAALGMRVLGNPYGNDPRIISGESGAVGLGVLAAVHYHPQRQSLMEKLA
LNKDAVVLVISTEGDTDVKHYREVVWEGKHAVA
3D structure
PDB4d9m Crystal Structure of Escherichia coli Diaminopropionate Ammonia-lyase Reveals Mechanism of Enzyme Activation and Catalysis
ChainB
Resolution2.5 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) K77 T376
Catalytic site (residue number reindexed from 1) K76 T362
Enzyme Commision number 4.3.1.15: diaminopropionate ammonia-lyase.
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 0JO B K77 T119 D120 N122 H123 G232 V233 G234 A235 M236 G288 L289 T376 E377 K76 T111 D112 N114 H115 G224 V225 G226 A227 M228 G274 L275 T362 E363
Gene Ontology
Molecular Function
GO:0008838 diaminopropionate ammonia-lyase activity
GO:0016829 lyase activity
GO:0030170 pyridoxal phosphate binding
GO:0042803 protein homodimerization activity

View graph for
Molecular Function
External links
PDB RCSB:4d9m, PDBe:4d9m, PDBj:4d9m
PDBsum4d9m
PubMed22505717
UniProtP66899|DPAL_ECOLI Diaminopropionate ammonia-lyase (Gene Name=ygeX)

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