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3F2R

Crystal structure of human choline kinase alpha in complex with hemicholinium-3

Functional Information from PDB Data
site_idAC1
Number of Residues10
DetailsBINDING SITE FOR RESIDUE HC6 A 603
ChainResidue
AASP306
ATYR440
AGLN308
ATYR333
ATYR354
APHE361
ATRP420
ATRP423
AGLU434
APHE435

site_idAC2
Number of Residues3
DetailsBINDING SITE FOR RESIDUE UNX A 606
ChainResidue
AGLU309
AGLU349
ATYR352

site_idAC3
Number of Residues10
DetailsBINDING SITE FOR RESIDUE HC6 B 603
ChainResidue
BASP306
BGLN308
BTYR333
BTYR354
BPHE361
BTRP420
BILE433
BGLU434
BPHE435
BTYR440

site_idAC4
Number of Residues3
DetailsBINDING SITE FOR RESIDUE UNX B 606
ChainResidue
BGLU309
BGLU349
BTYR352

site_idAC5
Number of Residues3
DetailsBINDING SITE FOR RESIDUE UNX A 1
ChainResidue
AHOH19
ATYR437
AMET438

site_idAC6
Number of Residues3
DetailsBINDING SITE FOR RESIDUE UNX B 2
ChainResidue
BARG270
BTYR437
BMET438

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues8
DetailsBINDING: BINDING => ECO:0000269|PubMed:17007874, ECO:0000269|PubMed:20299452, ECO:0007744|PDB:2CKP, ECO:0007744|PDB:3G15
ChainResidueDetails
AARG117
AARG146
AGLN207
AASP330
BARG117
BARG146
BGLN207
BASP330

site_idSWS_FT_FI2
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:17007874, ECO:0007744|PDB:2CKQ
ChainResidueDetails
AGLY119
BGLY119

site_idSWS_FT_FI3
Number of Residues2
DetailsBINDING: BINDING => ECO:0000305
ChainResidueDetails
AGLN308
BGLN308

site_idSWS_FT_FI4
Number of Residues2
DetailsMOD_RES: N6-acetyllysine => ECO:0000269|PubMed:34077757
ChainResidueDetails
ALYS247
BLYS247

site_idSWS_FT_FI5
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0000269|PubMed:34077757
ChainResidueDetails
ASER279
BSER279

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1l8t
ChainResidueDetails
AASP306
AARG146

site_idCSA2
Number of Residues1
DetailsAnnotated By Reference To The Literature 1l8t
ChainResidueDetails
BASP306

237992

PDB entries from 2025-06-25

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