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4Q6R

Crystal structure of human sphingosine-1-phosphate lyase in complex with inhibitor 6-[(2R)-4-(4-benzyl-7-chlorophthalazin-1-yl)-2-methylpiperazin-1-yl]pyridine-3-carbonitrile

Functional Information from GO Data
ChainGOidnamespacecontents
A0016830molecular_functioncarbon-carbon lyase activity
A0019752biological_processcarboxylic acid metabolic process
A0030170molecular_functionpyridoxal phosphate binding
B0016830molecular_functioncarbon-carbon lyase activity
B0019752biological_processcarboxylic acid metabolic process
B0030170molecular_functionpyridoxal phosphate binding
Functional Information from PDB Data
site_idAC1
Number of Residues10
DetailsBINDING SITE FOR RESIDUE SIN A 901
ChainResidue
ATHR148
B30J602
ATYR150
AHIS242
APHE290
ALLP353
AHOH1176
AHOH1177
BHIS174
BTYR387

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE GOL A 902
ChainResidue
AARG462
AASN465
ALYS518
ATHR519
ATHR520

site_idAC3
Number of Residues10
DetailsBINDING SITE FOR RESIDUE 30J A 903
ChainResidue
ALEU173
APRO175
AILE386
ATYR387
AALA388
BMET528
BVAL538
BLEU541
BSER542
BPHE545

site_idAC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE PO4 B 601
ChainResidue
AASN171
AHIS174
BTHR148
BTYR150
BLLP353
BHOH854

site_idAC5
Number of Residues10
DetailsBINDING SITE FOR RESIDUE 30J B 602
ChainResidue
AILE525
AVAL538
ALEU541
ASER542
APHE545
ASIN901
BLEU173
BILE386
BTYR387
BALA388

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsModified residue: {"description":"N6-acetyllysine; alternate","evidences":[{"source":"PubMed","id":"19608861","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues4
DetailsModified residue: {"description":"3'-nitrotyrosine","evidences":[{"source":"PubMed","id":"16777052","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

249697

PDB entries from 2026-02-25

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