Structure of PDB 6hqv Chain B

Receptor sequence

>6hqvB (length=1536) Species: 759272 (Thermochaetoides thermophila DSM 1495)

EPTRIAILGKEDIIVDHGIWLNFVAHDLLQTLPSSTYVLITDTNLYTTYV
PPFQAVFEAAAPRDVRLLTYAIPPGEYSKSRETKAEIEDWMLSHACTRDT
VIIALGGGVIGDMIGYVAATFMRGVRFVQVPTTLLAMVDSSIGGKTAIDT
PMGKNLIGAFWQPRRIYIDLAFLETLPVREFINGMAEVIKTAAIWNETEF
TALEENAAAILEAVRSKASSPAARLAPIRHILKRIVLGSARVKAEVVSAD
EREGGLRNLLNFGHSIGHAYEAILAPQVLHGECVAIGMVKEAELARYLGV
LRPSAVARLTKLIASYDLPTSVHDKRIAKLSAGKECPVDVLLQKMAVDKK
NEGRKKKIVLLSAIGKTYEKKATVVDDRAIRLVLSPSVRVTPGVPKGLSV
TVTPPGSKSISNRALVLAALGEGTTRIHGLLHSDDVQYMLAAIEQLHGAD
FSWEDAGEILVVTGKGGKLQASKEPLYLGNAGTASRFLTSVVALCAPSAV
SSTVLTGNARMKVRPIGALVDALRANGVGVKYLEKEKSLPVEVDAAGGFA
GGVIELAATVSSQYVSSILMAAPYAHQPVTLRLVGGKPISQPYIDMTIAM
MASFGIKVERSAEDPNTYLIPKGVYKNPPEYVVESDASSATYPLAVAAIT
GTTCTIPNIGSESLQGDARFAVEVLRPMGCAVEQTATSTTVTGPPIGTLK
AIPHVDMEPMTDAFLTAAVLAAVADGTTQITGIANQRVKECNRIAAMKDQ
LAKFGVQCNELEDGIEVIGKPYQELRNPVEGIYCYDDHRVAMSHSVLSTI
SPHPVLILERECTAKTWPGWWDILSQFFKVQLDGEEDPTGTDRSIFIVGM
RGAGKSTAGRWMSELLKRPLVDLDAELERREGMTIPEIIRGERGWEGFRQ
AELELLQDVIKNQSKGYIFSCGGGIVETEAARKLLIDYHKNGGPVLLVHR
DNIREVYERRKPWFYECSNLQYHSPHEDGSEALLQPPADFARFVKLIAGQ
STHLEDVRAKKHSFFVSLTVPNVADALDIIPRVVVGSDAVELRVDLLESY
EPEFVARQVALLRAAAQVPIVYTVRTQSQGGKFPDEDYDLALRLYQTGLR
SGVEYLDLEMTMPDHILQAVTDAKGFTSIIASHHDPQCKLSWKSGSWIPF
YNKALQYGDVIKLVGVAREMADNFALTNFKAKMLAAHDNKPMIALNMGTA
GKLSRVLNGFLTPVSHPALPSKAAPGQLSATEIRQALSLIGEIEPKSFYL
FGKPISASRSPALHNTLFYKTGLPHHYSRFETDEASKALESLIRSPDFGG
ASVTIPLKLDIMPLLDSATDAARTIGAVNTIIPQTRDGSTTTLVGDNTDW
RGMVHALLHSSGSGSVVQRTAAPRGAAMVVGSGGTARAAIYALHDLGFAP
IWIVARSEERVAELVRGFDGYDLRRMTSPHQGKDNMPSVVISTIPATQPI
DPSMREVIVEVLKHGHPSAEGKVLLEMAYQPPRTPLMTLAEDQGWRTVGG
LEVLAAQGWYQFQLWTGITPLYEEARAAVMGEDSVE

3D structure

• PDB: 6hqv Architecture and functional dynamics of the pentafunctional AROM complex.
• Chain: B
• Resolution: 3.0 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): R137 K159 E201 K257 E267 R271 N275 H278 H282 H294
• Catalytic site (residue number reindexed from 1): R123 K145 E187 K243 E253 R257 N261 H264 H268 H280
• Enzyme Commision number: 1.1.1.25: shikimate dehydrogenase (NADP(+)).
  2.5.1.19: 3-phosphoshikimate 1-carboxyvinyltransferase.
  2.7.1.71: shikimate kinase.
  4.2.1.10: 3-dehydroquinate dehydratase.
  4.2.3.4: 3-dehydroquinate synthase.

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	NAD	B	D56 N58 L59 E90 K93 G121 G122 V123 D126 T146 T147 L149 D153 S154 K168 T189 L190 P191 E194 H294	D42 N44 L45 E76 K79 G107 G108 V109 D112 T132 T133 L135 D139 S140 K154 T175 L176 P177 E180 H280
BS02	ZN	B	E201 H278 H294	E187 H264 H280
BS03	GLU	B	D153 K159 E201 K257 R271 N275 H278 H294	D139 K145 E187 K243 R257 N261 H264 H280
BS04	3DS	B	E1086 R1088 K1207 R1250 P1258 A1269	E1041 R1043 K1162 R1205 P1213 A1224
BS05	SKM	B	S1303 S1305 T1349 K1353 N1374 D1394 Y1524 Q1552	S1258 S1260 T1304 K1308 N1329 D1349 Y1479 Q1507
BS06	SKM	B	D900 G949 G950 R1005	D874 G923 G924 R960
BS07	SKM	B	R427 S576 Q577	R413 S562 Q563

Gene Ontology

Molecular Function

• GO:0003824 catalytic activity
• GO:0003855 3-dehydroquinate dehydratase activity
• GO:0003856 3-dehydroquinate synthase activity
• GO:0003866 3-phosphoshikimate 1-carboxyvinyltransferase activity
• GO:0004764 shikimate 3-dehydrogenase (NADP+) activity
• GO:0004765 shikimate kinase activity
• GO:0005524 ATP binding
• GO:0016301 kinase activity
• GO:0016491 oxidoreductase activity
• GO:0016765 transferase activity, transferring alkyl or aryl (other than methyl) groups
• GO:0016829 lyase activity
• GO:0046872 metal ion binding

Biological Process

• GO:0008652 amino acid biosynthetic process
• GO:0009073 aromatic amino acid family biosynthetic process
• GO:0009423 chorismate biosynthetic process
• GO:0016310 phosphorylation

Cellular Component

• GO:0005737 cytoplasm

External links

• PDB: RCSB:6hqv, PDBe:6hqv, PDBj:6hqv
• PDBsum: 6hqv
• PubMed: 32632294
• UniProt: G0S061