Structure of PDB 1kb0 Chain A Binding Site BS02

Receptor Information
>1kb0 Chain A (length=670) Species: 285 (Comamonas testosteroni) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
TGPAAQAAAAVQRVDGDFIRANAARTPDWPTIGVDYAETRYSRLDQINAA
NVKDLGLAWSYNLESTRGVEATPVVVDGIMYVSASWSVVHAIDTRTGNRI
WTYDPQIDRSTGFKGCCDVVNRGVALWKGKVYVGAWDGRLIALDAATGKE
VWHQNTFEGQKGSLTITGAPRVFKGKVIIGNGGAEYGVRGYITAYDAETG
ERKWRWFSVPGDPSKPFEDESMKRAARTWDPSGKWWEAGGGGTMWDSMTF
DAELNTMYVGTGNGSPWSHKVRSPKGGDNLYLASIVALDPDTGKYKWHYQ
ETPGDNWDYTSTQPMILADIKIAGKPRKVILHAPKNGFFFVLDRTNGKFI
SAKNFVPVNWASGYDKHGKPIGIAAARDGSKPQDAVPGPYGAHNWHPMSF
NPQTGLVYLPAQNVPVNLMDDKKWEFNQAGPGKPQSGTGWNTAKFFNAEP
PKSKPFGRLLAWDPVAQKAAWSVEHVSPWNGGTLTTAGNVVFQGTADGRL
VAYHAATGEKLWEAPTGTGVVAAPSTYMVDGRQYVSVAVGWGGVYGLAAR
ATERQGPGTVYTFVVGGKARMPETGQLLQGVKYDPAKVEAGTMLYVANCV
FCHGVPGVDRGGNIPNLGYMDASYIENLPNFVFKGPAMVRGMPDFTGKLS
GDDVESLKAFIQGTADAIRP
Ligand information
Ligand IDHEC
InChIInChI=1S/C34H34N4O4.Fe/c1-7-21-17(3)25-13-26-19(5)23(9-11-33(39)40)31(37-26)16-32-24(10-12-34(41)42)20(6)28(38-32)15-30-22(8-2)18(4)27(36-30)14-29(21)35-25;/h7-8,13-16H,9-12H2,1-6H3,(H,39,40)(H,41,42);/q-4;+4/b21-7?,22-8?,26-13-,29-14-,30-15-,31-16-;
InChIKeyHXQIYSLZKNYNMH-LJNAALQVSA-N
SMILES
SoftwareSMILES
ACDLabs 10.04O=C(O)CCC1=C(C2=CC6=C(C(=C/C)\C5=CC4=C(C(\C3=Cc7c(c(c8C=C1N2[Fe](N34)(N56)n78)CCC(=O)O)C)=C/C)C)C)C
OpenEye OEToolkits 1.5.0CC=C1C(=C2C=C3C(=CC)C(=C4N3[Fe]56N2C1=Cc7n5c(c(c7C)CCC(=O)O)C=C8N6C(=C4)C(=C8CCC(=O)O)C)C)C
CACTVS 3.341C\C=C1/C(=C2C=C3N4C(=Cc5n6c(C=C7N8C(=C(C)\C7=C/C)C=C1N2[Fe@@]468)c(C)c5CCC(O)=O)C(=C3C)CCC(O)=O)C
CACTVS 3.341CC=C1C(=C2C=C3N4C(=Cc5n6c(C=C7N8C(=C(C)C7=CC)C=C1N2[Fe]468)c(C)c5CCC(O)=O)C(=C3C)CCC(O)=O)C
FormulaC34 H34 Fe N4 O4
NameHEME C
ChEMBL
DrugBank
ZINC
PDB chain1kb0 Chain A Residue 802 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
Global viewLocal viewStructure summary

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PDB1kb0 Crystal structure of quinohemoprotein alcohol dehydrogenase from Comamonas testosteroni: structural basis for substrate oxidation and electron transfer.
Resolution1.44 Å
Binding residue
(original residue number in PDB)		N603 C604 C607 H608 L622 M625 F636 A642 R645 M647 P648 F650
Binding residue
(residue number reindexed from 1)		N598 C599 C602 H603 L617 M620 F631 A637 R640 M642 P643 F645
Annotation score1
Enzymatic activity
Catalytic site (original residue number in PDB) E185 N263 D308
Catalytic site (residue number reindexed from 1) E185 N263 D308
Enzyme Commision number 1.1.9.1: alcohol dehydrogenase (azurin).
Gene Ontology
Molecular Function
GO:0005509 calcium ion binding
GO:0009055 electron transfer activity
GO:0016491 oxidoreductase activity
GO:0016614 oxidoreductase activity, acting on CH-OH group of donors
GO:0020037 heme binding
GO:0046872 metal ion binding
Cellular Component
GO:0016020 membrane
GO:0030288 outer membrane-bounded periplasmic space
GO:0042597 periplasmic space

View graph for
Molecular Function
View graph for
Cellular Component
External links
PDB RCSB:1kb0, PDBe:1kb0, PDBj:1kb0
PDBsum1kb0
PubMed11714714
UniProtQ46444|QHED_COMTE Quinohemoprotein alcohol dehydrogenase (Gene Name=qheDH)

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