Structure of PDB 3gsb Chain B

Receptor sequence

>3gsbB (length=427) Species: 1131 (Synechococcus sp.)

FKTIKSDEIFAAAQKLMPGGVSSPVRAFKSVGGQPIVFDRVKDAYAWDVD
GNRYIDYVGTWGPAICGHAHPEVIEALKVAMEKGTSFGAPCALENVLAEM
VNDAVPSIEMVRFVNSGTEACMAVLRLMRAYTGRDKIIKFEGCYHGHADM
FLVKAGSGVATLGLPSSPGVPKKTTANTLTTPYNDLEAVKALFAENPGEI
AGVILEPIVGNSGFIVPDAGFLEGLREITLEHDALLVFDEVMTGFRIAYG
GVQEKFGVTPDLTTLGKIIGGGLPVGAYGGKREIMQLVAPAGPMYQAGTL
SGNPLAMTAGIKTLELLRQPGTYEYLDQITKRLSDGLLAIAQETGHAACG
GQVSGMFGFFFTEGPVHNYEDAKKSDLQKFSRFHRGMLEQGIYLAPSQFE
AGFTSLAHTEEDIDATLAAARTVMSAL

3D structure

• PDB: 3gsb Crystal structure of glutamate-1-semialdehyde aminomutase: an alpha2-dimeric vitamin B6-dependent enzyme with asymmetry in structure and active site reactivity.
• Chain: B
• Resolution: 3.0 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): V27 Y150 E212 D245 M248 K273 A407
• Catalytic site (residue number reindexed from 1): V21 Y144 E206 D239 M242 K267 A401
• 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	GAB	B	G304 T305	G298 T299
BS02	PMP	B	G123 T124 Y150 D245	G117 T118 Y144 D239

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:3gsb, PDBe:3gsb, PDBj:3gsb
• PDBsum: 3gsb
• PubMed: 9144156
• UniProt: P24630|GSA_SYNP6 Glutamate-1-semialdehyde 2,1-aminomutase (Gene Name=hemL)