Structure of PDB 2pan Chain F

Receptor sequence

>2panF (length=592) Species: 562 (Escherichia coli) [Search protein sequence]

AKMRAVDAAMYVLEKEGITTAFGVPGAAINPFYSAMRKHGGIRHILARHV
EGASHMAEGYTRATAGNIGVCLGTSGPAGTDMITALYSASADSIPILCIT
GQAPRARLHKEDFQAVDIEAIAKPVSKMAVTVREAALVPRVLQQAFHLMR
SGRPGPVLVDLPFDVQVAEIEFDPDMYEPLPVYKPAASRMQIEKAVEMLI
QAERPVIVAGGGVINADAAALLQQFAELTSVPVIPTLMGWGCIPDDHELM
AGMVGLQTAHRYGNATLLASDMVFGIGNRFANRHTGSVEKYTEGRKIVHI
DIEPTQIGRVLCPDLGIVSDAKAALTLLVEVAQEMQKAGRLPCRKEWVAD
CQQRKRTLLRKTHFDNVPVKPQRVYEEMNKAFGRDVCYVTTIGLSQIAAA
QMLHVFKDRHWINCGQAGPLGWTIPAALGVCAADPKRNVVAISGDFDFQF
LIEELAVGAQFNIPYIHVLVNNAYLGLIRQSQRAFDMDYCVQLAFENINS
SEVNGYGVDHVKVAEGLGCKAIRVFKPEDIAPAFEQAKALMAQYRVPVVV
EVILERVTNISMGSELDNVMEFEDIADNAADAPTETCFMHYE

3D structure

PDB

2pan Glyoxylate carboligase lacks the canonical active site glutamate of thiamine-dependent enzymes.

Chain

Resolution

2.7 Å

3D
structure

Catalytic site residues are labeled in the structure
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Enzymatic activity

Catalytic site (original residue number in PDB)	V25 G27 A28 A29 I30 V51 T75 F114 Q115 A116 F164 L257 H285 I393 G419 L421 D446 N473 Y475 L476 L478 I479 S482 R557
Catalytic site (residue number reindexed from 1)	V24 G26 A27 A28 I29 V50 T74 F113 Q114 A115 F163 L256 H284 I392 G418 L420 D445 N472 Y474 L475 L477 I478 S481 R556
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)
BS01	MG	F	D446 N473 Y475	D445 N472 Y474
BS02	MG	F	F451 L452 E454	F450 L451 E453
BS03	FAD	F	P155 G211 G212 G213 N216 T237 L238 M239 V255 G256 Q258 T259 G278 N279 R280 A282 R284 H285 D302 I303 Q307 D321 A322 Q397 G416	P154 G210 G211 G212 N215 T236 L237 M238 V254 G255 Q257 T258 G277 N278 R279 A281 R283 H284 D301 I302 Q306 D320 A321 Q396 G415
BS04	TPP	F	G394 L395 S396 L421 G445 D446 F447 D448 N473 Y475 L476 G477 L478 I479	G393 L394 S395 L420 G444 D445 F446 D447 N472 Y474 L475 G476 L477 I478

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

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Molecular Function

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Biological Process

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Cellular Component

External links

PDB	RCSB:2pan, PDBe:2pan, PDBj:2pan
PDBsum	2pan
PubMed	18176558
UniProt	P0AEP7\|GCL_ECOLI Glyoxylate carboligase (Gene Name=gcl)

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