Structure of PDB 5im3 Chain B

Receptor sequence
>5im3B (length=860) Species: 208964 (Pseudomonas aeruginosa PAO1) [Search protein sequence]
GQLRVIKRNGTVVPYTDDKITVAITKAFLAVEAAASSRIHDTVRRLTEQV
TATFKRRMPSGGTIHIEEIQDQVELALMRAGEQKVARDYVIYREARAAER
KNASIRITRADGSLSPLDMGRLNTIISEACEGLAEVDGALIERETLKNLY
DGVAEKDVNTALVMTARTLVEREPNYSYVTARLLMDTLRAEALGFLGVAE
SATHHEMAELYAKALPAYIEKGAEFELVDAKLKEFDLEKLGKAIDHERDQ
QFTYLGLQTLYDRYFIHKDGIRFELPQIFFMRVAMGLAIEEKDREARAIE
FYNLLSSFDYMSSTPTLFNAGTLRPQLSSCYLTTVPDDLSGIYGAIHDNA
MLSKFAGGLGNDWTPVRALGSYIKGTNGKSQGVVPFLKVVNDTAVAVNAV
CAYLETWHLDIEEFLELRKNTGDDRRRTHDMNTANWIPDLFMKRVFDDGS
WTLFSPSDVPDLHDLYGKAFEERYEYYEALASYGKLKLHKVVQAKDLWRK
MLSMLFETGHPWLTFKDPCNLRSPQQHVGVVHSSNLCTEITLNTNKDEIA
VCNLGSINLVNHIVDGKLDTAKLEKTVKTAVRMLDNVIDINYYSVPQAQN
SNFKHRPVGLGIMGFQDALYLQHIPYGSDAAIAFADQSMEAISYYAIQAS
CDLADERGAYQTFQGSLWSQGILPIDSEKKLIEERGAKYIEVDLSETLDW
APLRERVQKGIRNSNIMAIAPTATIANITGVSQSIEPTYQNLYVKSNLSG
EFTVINPYLVRDLKARGLWDPVMVNDLKYYDGSVQQIERIPQDLKDLYAT
AFEVETRWIVEAASRRQKWIDQAQSLNLYIAGASGKKLDVTYRMAWFRGL
KTTYYLRALA
3D structure
PDB5im3 Structural Mechanism of Allosteric Activity Regulation in a Ribonucleotide Reductase with Double ATP Cones.
ChainB
Resolution2.298 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) C373 N585 C587 E589 C602 Y904 Y905
Catalytic site (residue number reindexed from 1) C330 N535 C537 E539 C552 Y854 Y855
Enzyme Commision number 1.17.4.1: ribonucleoside-diphosphate reductase.
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 DTP B D380 D381 L382 I385 R410 I416 K417 D337 D338 L339 I342 R367 I373 K374 MOAD: Kd~1.5uM
BS02 DTP B K397 A439 V440 K354 A396 V397 MOAD: Kd~1.5uM
BS03 DTP B K36 R37 Y44 T45 K48 I49 I101 Q102 K7 R8 Y15 T16 K19 I20 I69 Q70 MOAD: Kd~1.5uM
BS04 DTP B A52 K55 A56 D120 Y121 Y124 R128 R132 A23 K26 A27 D88 Y89 Y92 R96 R100 MOAD: Kd~1.5uM
Gene Ontology
Molecular Function
GO:0004748 ribonucleoside-diphosphate reductase activity, thioredoxin disulfide as acceptor
GO:0005524 ATP binding
GO:0016491 oxidoreductase activity
Biological Process
GO:0009263 deoxyribonucleotide biosynthetic process
Cellular Component
GO:0005971 ribonucleoside-diphosphate reductase complex

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Molecular Function

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Biological Process

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Cellular Component
External links
PDB RCSB:5im3, PDBe:5im3, PDBj:5im3
PDBsum5im3
PubMed27133024
UniProtQ9I4I1

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