Structure of PDB 2hp1 Chain B

Receptor sequence

>2hp1B (length=398) Species: 269084 (Synechococcus elongatus PCC 6301)

FKTIKSDEIFAAAQKLMPGGVSSPVRAFKSVGGQPIVFDRVKDAYAWDVD
GNRYIDYVGTWGPAICGHAHPEVIEALKVAMEKGTSFGAPCALENVLAEM
VNDAVPSIEMVRFVNSGTEACMAVLRIMRAYTGRDKIIKFEGCYHGHNTL
TTPYNDLEAVKALFAENPGEIAGVILEPIVGNSGFIVPDAGFLEGLREIT
LEHDALLVFDEVMTGFRIAYGGVQEKFGVTPDLTTLGKIIGGGLPVGAYG
GKREIMQLVAPAGPMYQAGTLSGNPLAMTAGIKTLELLRQPGTYEYLDQI
TKRLSDGLLAIAQETGHAACGGQVSGMFGFFFTEGPVHNYEDAKKSDLQK
FSRFHRGMLEQGIYLAPSQFEAGFTSLAHTEEDIDATLAAARTVMSAL

3D structure

• PDB: 2hp1 Intersubunit signaling in glutamate-1-semialdehyde-aminomutase.
• Chain: B
• Resolution: 2.08 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): V2027 Y2150 E2212 D2245 M2248 K2273 A2407
• Catalytic site (residue number reindexed from 1): V21 Y144 E177 D210 M213 K238 A372
• 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	EA5	B	G2304 T2305	G269 T270
BS02	PLP	B	S2122 G2123 T2124 Y2150 E2212 N2217 D2245 V2247 M2248 K2273	S116 G117 T118 Y144 E177 N182 D210 V212 M213 K238
BS03	HOZ	B	S2029 V2031 R2032 W2067 Y2150	S23 V25 R26 W61 Y144

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:2hp1, PDBe:2hp1, PDBj:2hp1
• PDBsum: 2hp1
• PubMed: 16954186
• UniProt: P24630|GSA_SYNP6 Glutamate-1-semialdehyde 2,1-aminomutase (Gene Name=hemL)