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3A1E

Crystal structure of the P- and N-domains of His462Gln mutant CopA, a copper-transporting P-type ATPase, bound with AMPPCP-Mg

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0005215molecular_functiontransporter activity
A0005524molecular_functionATP binding
A0016020cellular_componentmembrane
A0016887molecular_functionATP hydrolysis activity
B0000166molecular_functionnucleotide binding
B0005215molecular_functiontransporter activity
B0005524molecular_functionATP binding
B0016020cellular_componentmembrane
B0016887molecular_functionATP hydrolysis activity
Functional Information from PDB Data
site_idAC1
Number of Residues23
DetailsBINDING SITE FOR RESIDUE ACP A 997
ChainResidue
AASP424
AVAL500
AGLY501
AASN502
AVAL532
ATHR572
AGLY573
AASP574
APRO597
ALYS600
AMG998
ALYS425
AHOH1121
AHOH1127
AHOH1141
AHOH1150
ATHR426
AGLU457
AGLN462
AILE464
AGLY490
AGLU491
AGLY492

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE MG A 998
ChainResidue
AASP424
ATHR426
AACP997
AHOH1001

site_idAC3
Number of Residues16
DetailsBINDING SITE FOR RESIDUE ACP B 997
ChainResidue
BASP424
BLYS425
BTHR426
BGLU457
BGLN462
BGLY490
BGLU491
BVAL493
BVAL500
BGLY501
BASN502
BTHR572
BGLY573
BASP574
BLYS600
BHOH1391

Functional Information from PROSITE/UniProt
site_idPS00154
Number of Residues7
DetailsATPASE_E1_E2 E1-E2 ATPases phosphorylation site. DKTGTLT
ChainResidueDetails
AASP424-THR430

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: 4-aspartylphosphate intermediate => ECO:0000250
ChainResidueDetails
AASP424
BASP424

site_idSWS_FT_FI2
Number of Residues4
DetailsBINDING: BINDING => ECO:0000255
ChainResidueDetails
AGLU457
AGLY490
BGLU457
BGLY490

site_idSWS_FT_FI3
Number of Residues4
DetailsBINDING:
ChainResidueDetails
AASP618
AASP622
BASP618
BASP622

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PDB entries from 2024-11-06

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