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6R5E

Crystal structure of the Pri1 subunit of human primase bound to 2F-ATP

Functional Information from GO Data
ChainGOidnamespacecontents
A0000287molecular_functionmagnesium ion binding
A0000428cellular_componentDNA-directed RNA polymerase complex
A0003896molecular_functionDNA primase activity
A0005515molecular_functionprotein binding
A0005654cellular_componentnucleoplasm
A0005658cellular_componentalpha DNA polymerase:primase complex
A0006260biological_processDNA replication
A0006269biological_processDNA replication, synthesis of primer
A0006270biological_processDNA replication initiation
A0008270molecular_functionzinc ion binding
A0016020cellular_componentmembrane
A0016779molecular_functionnucleotidyltransferase activity
A0032553molecular_functionribonucleotide binding
A0046872molecular_functionmetal ion binding
A1990077cellular_componentprimosome complex
E0000287molecular_functionmagnesium ion binding
E0000428cellular_componentDNA-directed RNA polymerase complex
E0003896molecular_functionDNA primase activity
E0005515molecular_functionprotein binding
E0005654cellular_componentnucleoplasm
E0005658cellular_componentalpha DNA polymerase:primase complex
E0006260biological_processDNA replication
E0006269biological_processDNA replication, synthesis of primer
E0006270biological_processDNA replication initiation
E0008270molecular_functionzinc ion binding
E0016020cellular_componentmembrane
E0016779molecular_functionnucleotidyltransferase activity
E0032553molecular_functionribonucleotide binding
E0046872molecular_functionmetal ion binding
E1990077cellular_componentprimosome complex
Functional Information from PDB Data
site_idAC1
Number of Residues4
Detailsbinding site for residue ZN A 501
ChainResidue
ACYS121
ACYS122
ACYS128
ACYS131

site_idAC2
Number of Residues5
Detailsbinding site for residue MN A 502
ChainResidue
AASP109
AASP111
AMN503
AJSQ504
AHOH674

site_idAC3
Number of Residues7
Detailsbinding site for residue MN A 503
ChainResidue
AASP109
AASP111
AASP306
AMN502
AJSQ504
AHOH686
AHOH756

site_idAC4
Number of Residues17
Detailsbinding site for residue JSQ A 504
ChainResidue
AASP79
AASP109
AASP111
ASER160
AARG162
AARG163
AHIS166
AHIS315
ALEU316
ALEU317
ALYS318
AHIS324
AMN502
AMN503
AHOH674
AHOH686
AHOH750

site_idAC5
Number of Residues5
Detailsbinding site for residue EDO A 505
ChainResidue
ATHR349
ASER351
EASP149
EPHE150
ETYR188

site_idAC6
Number of Residues3
Detailsbinding site for residue EDO A 506
ChainResidue
AASP335
APHE342
AHOH739

site_idAC7
Number of Residues4
Detailsbinding site for residue EDO A 507
ChainResidue
AGLU187
AHOH627
AHOH694
EARG355

site_idAC8
Number of Residues3
Detailsbinding site for residue EDO A 508
ChainResidue
AASP126
AILE127
AHOH611

site_idAC9
Number of Residues5
Detailsbinding site for residue EDO A 509
ChainResidue
ALYS153
AHIS154
AARG155
AASN401
AHOH621

site_idAD1
Number of Residues4
Detailsbinding site for residue EDO A 510
ChainResidue
ALYS130
AASN230
AHOH608
AHOH685

site_idAD2
Number of Residues4
Detailsbinding site for residue ZN E 501
ChainResidue
ECYS121
ECYS122
ECYS128
ECYS131

site_idAD3
Number of Residues5
Detailsbinding site for residue MN E 502
ChainResidue
EASP109
EASP111
EMN503
EJSQ504
EHOH685

site_idAD4
Number of Residues7
Detailsbinding site for residue MN E 503
ChainResidue
EASP109
EASP111
EASP306
EMN502
EJSQ504
EHOH745
EHOH751

site_idAD5
Number of Residues20
Detailsbinding site for residue JSQ E 504
ChainResidue
AARG278
ETYR54
EARG56
ELYS77
EASP79
EASP109
EASP111
ESER160
EARG162
EARG163
EHIS166
EHIS315
ELEU316
ELEU317
ELYS318
EHIS324
EMN502
EMN503
EHOH647
EHOH745

site_idAD6
Number of Residues5
Detailsbinding site for residue EDO E 505
ChainResidue
AASP149
APHE150
ATYR188
ETHR349
ESER351

site_idAD7
Number of Residues3
Detailsbinding site for residue EDO E 506
ChainResidue
EASP343
EPHE345
ASER173

site_idAD8
Number of Residues5
Detailsbinding site for residue EDO E 507
ChainResidue
EPHE342
EASP343
ETHR346
EVAL347
ETYR391

site_idAD9
Number of Residues5
Detailsbinding site for residue EDO E 508
ChainResidue
ASER205
ELEU357
EASP358
EHOH601
EHOH629

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues6
DetailsACT_SITE: ACT_SITE => ECO:0000255
ChainResidueDetails
AGLU44
AASP109
AASP111
EGLU44
EASP109
EASP111

site_idSWS_FT_FI2
Number of Residues6
DetailsBINDING: BINDING => ECO:0000269|PubMed:31479243, ECO:0007744|PDB:6R4S
ChainResidueDetails
AASP109
AASP111
AASP306
EASP109
EASP111
EASP306

site_idSWS_FT_FI3
Number of Residues8
DetailsBINDING: BINDING => ECO:0000269|PubMed:24043831, ECO:0000269|PubMed:25550159, ECO:0000269|PubMed:26975377, ECO:0000269|PubMed:31479243
ChainResidueDetails
ACYS121
ACYS122
ACYS128
ACYS131
ECYS121
ECYS122
ECYS128
ECYS131

site_idSWS_FT_FI4
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:24043831, ECO:0000269|PubMed:24239947, ECO:0000269|PubMed:31479243
ChainResidueDetails
ASER160
ESER160

site_idSWS_FT_FI5
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:24043831, ECO:0000269|PubMed:31479243
ChainResidueDetails
AHIS315
EHIS315

site_idSWS_FT_FI6
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:31479243
ChainResidueDetails
AHIS324
EHIS324

site_idSWS_FT_FI7
Number of Residues2
DetailsMOD_RES: N-acetylmethionine => ECO:0007744|PubMed:22223895
ChainResidueDetails
AMET1
EMET1

224004

PDB entries from 2024-08-21

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