Structure of PDB 3fqa Chain B

Receptor sequence

>3fqaB (length=426) Species: 269084 (Synechococcus elongatus PCC 6301)

KTIKSDEIFAAAQKLMPGGVSSPVRAFKSVGGQPIVFDRVKDAYAWDVDG
NRYIDYVGTWGPAICGHAHPEVIEALKVAMEKGTSFGAPCALENVLAEMV
NDAVPSIEMVRFVNSGTEACMAVLRLMRAYTGRDKIIKFEGCYHGHADMF
LVKAGSGVATLGLPSSPGVPKKTTANTLTTPYNDLEAVKALFAENPGEIA
GVILEPIVGNSGFIVPDAGFLEGLREITLEHDALLVFDEVITGFRIAYGG
VQEKFGVTPDLTTLGKIIGGGLPVGAYGGKREIMQLVAPAGPMYQAGTLS
GNPLAMTAGIKTLELLRQPGTYEYLDQITKRLSDGLLAIAQETGHAACGG
QVSGMFGFFFTEGPVHNYEDAKKSDLQKFSRFHRGMLEQGIYLAPSQFEA
GFTSLAHTEEDIDATLAAARTVMSAL

3D structure

• PDB: 3fqa Absence of a catalytic water confers resistance to the neurotoxin gabaculine.
• Chain: B
• Resolution: 2.35 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): V2027 Y2150 E2212 D2245 I2248 K2273 A2407
• Catalytic site (residue number reindexed from 1): V20 Y143 E205 D238 I241 K266 A400
• Enzyme Commision number: 5.4.3.8: glutamate-1-semialdehyde 2,1-aminomutase.

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	PMP	B	G2304 T2305	G297 T298
BS02	GAB	B	A2303 G2304 T2305	A296 G297 T298	PDBbind-CN: -logKd/Ki=0.49,IC50=320mM
BS03	PMP	B	G2123 T2124 Y2150 E2212 N2217 D2245 V2247 I2248 K2273	G116 T117 Y143 E205 N210 D238 V240 I241 K266

Gene Ontology

Molecular Function

• GO:0008483 transaminase activity
• GO:0016853 isomerase activity
• GO:0030170 pyridoxal phosphate binding
• GO:0042286 glutamate-1-semialdehyde 2,1-aminomutase activity

Biological Process

• GO:0006782 protoporphyrinogen IX biosynthetic process
• GO:0015995 chlorophyll biosynthetic process
• GO:0033014 tetrapyrrole biosynthetic process

Cellular Component

• GO:0005737 cytoplasm

External links

• PDB: RCSB:3fqa, PDBe:3fqa, PDBj:3fqa
• PDBsum: 3fqa
• PubMed: 19786580
• UniProt: P24630|GSA_SYNP6 Glutamate-1-semialdehyde 2,1-aminomutase (Gene Name=hemL)