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2HOY

Inter-subunit signaling in GSAM

Functional Information from GO Data
ChainGOidnamespacecontents
A0005737cellular_componentcytoplasm
A0006779biological_processporphyrin-containing compound biosynthetic process
A0006782biological_processprotoporphyrinogen IX biosynthetic process
A0008483molecular_functiontransaminase activity
A0015995biological_processchlorophyll biosynthetic process
A0016853molecular_functionisomerase activity
A0030170molecular_functionpyridoxal phosphate binding
A0033014biological_processtetrapyrrole biosynthetic process
A0042286molecular_functionglutamate-1-semialdehyde 2,1-aminomutase activity
B0005737cellular_componentcytoplasm
B0006779biological_processporphyrin-containing compound biosynthetic process
B0006782biological_processprotoporphyrinogen IX biosynthetic process
B0008483molecular_functiontransaminase activity
B0015995biological_processchlorophyll biosynthetic process
B0016853molecular_functionisomerase activity
B0030170molecular_functionpyridoxal phosphate binding
B0033014biological_processtetrapyrrole biosynthetic process
B0042286molecular_functionglutamate-1-semialdehyde 2,1-aminomutase activity
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE PO4 A 601
ChainResidue
ASER122
AGLY123
ATHR124
AHOH670
BTHR305
BHOH704

site_idAC2
Number of Residues7
DetailsBINDING SITE FOR RESIDUE PO4 B 602
ChainResidue
BGLY123
BTHR124
BHOH644
BHOH848
ATHR305
ALEU306
BSER122

Functional Information from PROSITE/UniProt
site_idPS00600
Number of Residues37
DetailsAA_TRANSFER_CLASS_3 Aminotransferases class-III pyridoxal-phosphate attachment site. LVfDEVmt.GF.RiAyggvqekfgvtp....DLTtlGKiigGG
ChainResidueDetails
ALEU242-GLY278

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsMOD_RES: N6-(pyridoxal phosphate)lysine
ChainResidueDetails
AILE274
BILE274

Catalytic Information from CSA
site_idMCSA1
Number of Residues3
DetailsM-CSA 195
ChainResidueDetails
AHIS151steric role
AGLU246electrostatic stabiliser, hydrogen bond acceptor
AILE274covalently attached, electron pair acceptor, electron pair donor, hydrogen bond acceptor, hydrogen bond donor, nucleofuge, nucleophile, proton acceptor, proton donor

site_idMCSA2
Number of Residues3
DetailsM-CSA 195
ChainResidueDetails
BHIS151steric role
BGLU246electrostatic stabiliser, hydrogen bond acceptor
BILE274covalently attached, electron pair acceptor, electron pair donor, hydrogen bond acceptor, hydrogen bond donor, nucleofuge, nucleophile, proton acceptor, proton donor

218853

PDB entries from 2024-04-24

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