Structure of PDB 2hoz Chain A

Receptor sequence

>2hozA (length=427) Species: 269084 (Synechococcus elongatus PCC 6301)

FKTIKSDEIFAAAQKLMPGGVSSPVRAFKSVGGQPIVFDRVKDAYAWDVD
GNRYIDYVGTWGPAICGHAHPEVIEALKVAMEKGTSFGAPCALENVLAEM
VNDAVPSIEMVRFVNSGTEACMAVLRIMRAYTGRDKIIKFEGCYHGHADM
FLVKAGSGVATLGLPSSPGVPKKTTANTLTTPYNDLEAVKALFAENPGEI
AGVILEPIVGNSGFIVPDAGFLEGLREITLEHDALLVFDEVMTGFRIAYG
GVQEKFGVTPDLTTLGKIIGGGLPVGAYGGKREIMQLVAPAGPMYQAGTL
SGNPLAMTAGIKTLELLRQPGTYEYLDQITKRLSDGLLAIAQETGHAACG
GQVSGMFGFFFTEGPVHNYEDAKKSDLQKFSRFHRGMLEQGIYLAPSQFE
AGFTSLAHTEEDIDATLAAARTVMSAL

3D structure

• PDB: 2hoz Intersubunit signaling in glutamate-1-semialdehyde-aminomutase.
• Chain: A
• Resolution: 2.2 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): V1027 Y1150 D1245 M1248 K1273 A1407
• Catalytic site (residue number reindexed from 1): V21 Y144 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	PMP	A	G1123 T1124 Y1150 H1151 G1152 E1212 N1217 D1245	G117 T118 Y144 H145 G146 E206 N211 D239
BS02	HOZ	A	E1147 G1162 S1163 P1188 N1374 E1376 K1379	E141 G156 S157 P182 N368 E370 K373
BS03	PMP	A	G1304 T1305	G298 T299

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:2hoz, PDBe:2hoz, PDBj:2hoz
• PDBsum: 2hoz
• PubMed: 16954186
• UniProt: P24630|GSA_SYNP6 Glutamate-1-semialdehyde 2,1-aminomutase (Gene Name=hemL)