Structure of PDB 2yg3 Chain A

Receptor sequence
>2yg3A (length=449) Species: 1833 (Rhodococcus erythropolis) [Search protein sequence]
PTLQRDVAIVGAGPSGLAAATALRKAGLSVAVIEARDRVGGRTWTDTIDG
AVLEIGGQWVSPDQTALISLLDELGLKTFERYREGESVYISSAGERTRYT
GDSFPTNETTKKEMDRLIDEMDDLAAQIGAEEPWAHPLARDLDTVSFKQW
LINQSDDAEARDNIGLFIAGGMLTKPAHSFSALQAVLMAASAGSFSHLVD
EDFILDKRVIGGMQQVSIRMAEALGDDVFLNAPVRTVKWNESGATVLADG
DIRVEASRVILAVPPNLYSRISYDPPLPRRQHQMHQHQSLGLVIKVHAVY
ETPFWREDGLSGTGFGASEVVQEVYDNTNHEDDRGTLVAFVSDEKADAMF
ELSAEERKATILASLARYLGPKAEEPVVYYESDWGSEEWTRGAYAASFDL
GGLHRYGADSRTPVGPIHFSCSDIAAEGYQHVDGAVRMGQRTAADIIAR
3D structure
PDB2yg3 Structure-Based Redesign of Cofactor Binding in Putrescine Oxidase.
ChainA
Resolution2.0 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) S62 S197 K296
Catalytic site (residue number reindexed from 1) S61 S196 K295
Enzyme Commision number 1.4.3.10: putrescine oxidase.
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 FAD A V11 G12 G14 P15 S16 E35 A36 R37 G42 R43 G57 G58 Q59 W60 V235 V264 W385 W390 Y395 C422 S423 Q431 H432 V433 A436 V10 G11 G13 P14 S15 E34 A35 R36 G41 R42 G56 G57 Q58 W59 V234 V263 W384 W389 Y394 C421 S422 Q430 H431 V432 A435
Gene Ontology
Molecular Function
GO:0000166 nucleotide binding
GO:0016491 oxidoreductase activity

View graph for
Molecular Function
External links
PDB RCSB:2yg3, PDBe:2yg3, PDBj:2yg3
PDBsum2yg3
PubMed21486042
UniProtB0F9F6

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