Structure of PDB 8i08 Chain A

Receptor sequence

>8i08A (length=594) Species: 83333 (Escherichia coli K-12)

GMAKMRAVDAAMYVLEKEGITTAFGVPGAAINPFYSAMRKHGGIRHILAR
HVEGASHMAEGYTRATAGNIGVCLGTSGPAGTDMITALYSASADSIPILC
ITGQAPRARLHKEDFQAVDIEAIAKPVSKMAVTVREAALVPRVLQQAFHL
MRSGRPGPVLVDLPFDVQVAEIEFDPDMYEPLPVYKPAASRMQIEKAVEM
LIQAERPVIVAGGGVINADAAALLQQFAELTSVPVIPTLMGWGCIPDDHE
LMAGMVGLQTAHRYGNATLLASDMVFGIGNRFAQRHTGSVEKYTEGRKIV
HIDIEPTQIGRVLCPDLGIVSDAKAALTLLVEVAQEMQKAGRLPCRKEWV
ADCQQRKRTLLRKTHFDNVPVKPQRVYEEMNKAFGRDVCYVTTIGLSQIA
AAQMLHVFKDRHWINCGQAGPLGWTIPAALGVCAADPKRNVVAISGDFDF
QFLIEELAVGAQFNIPYIHVLVNNAYLGMIRQSQMAFDLDYCVQLAFENI
NSSEVNGYGVDHVKVAEGLGCKAIRVFKPEDIAPAFEQAKALMAQYRVPV
VVEVILERVTNISMGSELDNVMEFEDIADNAADAPTETCFMHYE

3D structure

• PDB: 8i08 Engineering of two thiamine diphosphate-dependent enzymes for the regioselective condensation of C1-formaldehyde into C4-erythrulose
• Chain: A
• Resolution: 1.91 Å

Enzymatic activity

• Enzyme Commision number: 4.1.1.47: tartronate-semialdehyde 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	FAD	A	R154 P155 G211 G212 G213 N216 T237 L238 M239 V255 G256 Q258 T259 G278 N279 R280 R284 H285 D302 I303 Q307 D321 A322 G416	R155 P156 G212 G213 G214 N217 T238 L239 M240 V256 G257 Q259 T260 G279 N280 R281 R285 H286 D303 I304 Q308 D322 A323 G417
BS02	TPP	A	G394 L395 S396 L421 G445 D446 F447 D448 N473 Y475 L476 G477 M478 I479	G395 L396 S397 L422 G446 D447 F448 D449 N474 Y476 L477 G478 M479 I480
BS03	MG	A	D446 N473 Y475	D447 N474 Y476
BS04	MG	A	F451 L452 E454	F452 L453 E455
BS05	UQ0	A	Q353 C588	Q354 C589
BS06	UQ0	A	Y490 C491	Y491 C492

Gene Ontology

Molecular Function

• GO:0000287 magnesium ion binding
• GO:0003824 catalytic activity
• GO:0009028 tartronate-semialdehyde synthase activity
• GO:0016829 lyase activity
• GO:0030976 thiamine pyrophosphate binding
• GO:0042802 identical protein binding
• GO:0050660 flavin adenine dinucleotide binding
• GO:0071949 FAD binding

Biological Process

• GO:0009097 isoleucine biosynthetic process
• GO:0009099 L-valine biosynthetic process
• GO:0009436 glyoxylate catabolic process
• GO:0019752 carboxylic acid metabolic process
• GO:0046296 glycolate catabolic process

Cellular Component

• GO:0005948 acetolactate synthase complex

External links

• PDB: RCSB:8i08, PDBe:8i08, PDBj:8i08
• PDBsum: 8i08
• PubMed: 37890751
• UniProt: P0AEP7|GCL_ECOLI Glyoxylate carboligase (Gene Name=gcl)