Structure of PDB 2hoz Chain B

Receptor sequence
>2hozB (length=420) Species: 269084 (Synechococcus elongatus PCC 6301) [Search protein sequence]
FKTIKSDEIFAAAQKLMPGGVSSPVRAFKSVGGQPIVFDRVKDAYAWDVD
GNRYIDYVGTWGPAICGHAHPEVIEALKVAMEKGTSFGAPCALENVLAEM
VNDAVPSIEMVRFVNSGTEACMAVLRIMRAYTGRDKIIKFEGCYHGHADM
FLVKAGLPSSPGVPKKTTANTLTTPYNDLEAVKALFAENPGEIAGVILEP
IVGNSGFIVPDAGFLEGLREITLEHDALLVFDEVMTGFRIAYGGVQEKFG
VTPDLTTLGKIIGGGLPVGAYGGKREIMQLVAPAGPMYQAGTLSGNPLAM
TAGIKTLELLRQPGTYEYLDQITKRLSDGLLAIAQETGHAACGGQVSGMF
GFFFTEGPVHNYEDAKKSDLQKFSRFHRGMLEQGIYLAPSQFEAGFTSLA
HTEEDIDATLAAARTVMSAL
3D structure
PDB2hoz Intersubunit signaling in glutamate-1-semialdehyde-aminomutase.
ChainB
Resolution2.2 Å
3D
structure
Catalytic site residues are labeled in the structure
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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 E199 D232 M235 K260 A394
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 G291 T292
BS02 PMP B G2123 T2124 Y2150 H2151 G2152 E2212 N2217 D2245 G117 T118 Y144 H145 G146 E199 N204 D232
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

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:2hoz, PDBe:2hoz, PDBj:2hoz
PDBsum2hoz
PubMed16954186
UniProtP24630|GSA_SYNP6 Glutamate-1-semialdehyde 2,1-aminomutase (Gene Name=hemL)

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