Structure of PDB 5im3 Chain A

Receptor sequence
>5im3A (length=874) Species: 208964 (Pseudomonas aeruginosa PAO1) [Search protein sequence]
LRVIKRNGTVVPYTDDKITVAITKAFLAVEGGTAAASSRIHDTVRRLTEQ
VTATFKRRMPSGGTIHIEEIQDQVELALMRAGEQKVARDYVIYREARAAE
RKNAGAASDVAQPHPSIRITRADGSLSPLDMGRLNTIISEACEGLAEVDG
ALIERETLKNLYDGVAEKDVNTALVMTARTLVEREPNYSYVTARLLMDTL
RAEALGFLGVAESATHHEMAELYAKALPAYIEKGAEFELVDAKLKEFDLE
KLGKAIDHERDQQFTYLGLQTLYDRYFIHKDGIRFELPQIFFMRVAMGLA
IEEKDREARAIEFYNLLSSFDYMSSTPTLFNAGTLRPQLSSCYLTTVPDD
LSGIYGAIHDNAMLSKFAGGLGNDWTPVRALGSYIKGTNGKSQGVVPFLK
VVNDTAVAVNAVCAYLETWHLDIEEFLELRKNTGDDRRRTHDMNTANWIP
DLFMKRVFDDGSWTLFSPSDVPDLHDLYGKAFEERYEYYEALASYGKLKL
HKVVQAKDLWRKMLSMLFETGHPWLTFKDPCNLRSPQQHVGVVHSSNLCT
EITLNTNKDEIAVCNLGSINLVNHIVDGKLDTAKLEKTVKTAVRMLDNVI
DINYYSVPQAQNSNFKHRPVGLGIMGFQDALYLQHIPYGSDAAIAFADQS
MEAISYYAIQASCDLADERGAYQTFQGSLWSQGILPIDSEKKLIEERGAK
YIEVDLSETLDWAPLRERVQKGIRNSNIMAIAPTATIANITGVSQSIEPT
YQNLYVKSNLSGEFTVINPYLVRDLKARGLWDPVMVNDLKYYDGSVQQIE
RIPQDLKDLYATAFEVETRWIVEAASRRQKWIDQAQSLNLYIAGASGKKL
DVTYRMAWFRGLKTTYYLRALAAT
3D structure
PDB5im3 Structural Mechanism of Allosteric Activity Regulation in a Ribonucleotide Reductase with Double ATP Cones.
ChainA
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) C342 N547 C549 E551 C564 Y866 Y867
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 A V34 K36 Y44 T45 K48 I98 I101 Q102 V3 K5 Y13 T14 K17 I67 I70 Q71 MOAD: Kd~1.5uM
PDBbind-CN: -logKd/Ki=5.82,Kd~1.5uM
BS02 DTP A A52 K55 A59 Q102 D120 Y121 Y124 A21 K24 A28 Q71 D89 Y90 Y93 MOAD: Kd~1.5uM
PDBbind-CN: -logKd/Ki=5.82,Kd~1.5uM
BS03 DTP A K397 A439 V440 K366 A408 V409 MOAD: Kd~1.5uM
PDBbind-CN: -logKd/Ki=5.82,Kd~1.5uM
BS04 DTP A D380 D381 L382 I385 R410 I416 D349 D350 L351 I354 R379 I385 MOAD: Kd~1.5uM
PDBbind-CN: -logKd/Ki=5.82,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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