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5LXX

High-resolution structure of human collapsin response mediator protein 2

Functional Information from GO Data
ChainGOidnamespacecontents
A0005737cellular_componentcytoplasm
A0016787molecular_functionhydrolase activity
A0016810molecular_functionhydrolase activity, acting on carbon-nitrogen (but not peptide) bonds
B0005737cellular_componentcytoplasm
B0016787molecular_functionhydrolase activity
B0016810molecular_functionhydrolase activity, acting on carbon-nitrogen (but not peptide) bonds
Functional Information from PDB Data
site_idAC1
Number of Residues5
Detailsbinding site for residue SO4 A 501
ChainResidue
AMET83
ATHR84
AGLN340
AHOH717
BARG487

site_idAC2
Number of Residues3
Detailsbinding site for residue SO4 A 502
ChainResidue
AARG124
AHOH603
AHOH915

site_idAC3
Number of Residues7
Detailsbinding site for residue SO4 A 503
ChainResidue
ASER292
ALYS297
AHOH664
AHOH959
AHOH987
AHOH1061
AHIS289

site_idAC4
Number of Residues12
Detailsbinding site for residue SO4 A 504
ChainResidue
AARG400
AHOH619
AHOH631
AHOH784
AHOH862
AHOH964
AHOH974
AHOH978
BARG400
BALA402
BHOH912
BHOH964

site_idAC5
Number of Residues16
Detailsbinding site for residue BTB A 505
ChainResidue
AARG75
AMET78
APRO79
AASP80
ATYR167
APHE170
AARG173
APHE174
AGLU353
AHOH606
AHOH629
AHOH657
AHOH691
AHOH714
AHOH728
AHOH1031

site_idAC6
Number of Residues6
Detailsbinding site for residue SO4 B 501
ChainResidue
BHIS289
BSER292
BLYS297
BHOH652
BHOH986
BHOH1044

site_idAC7
Number of Residues15
Detailsbinding site for residue BTB B 502
ChainResidue
BARG75
BMET78
BPRO79
BASP80
BTYR167
BPHE170
BARG173
BPHE174
BGLU353
BHOH603
BHOH637
BHOH662
BHOH683
BHOH713
BHOH752

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsMOD_RES: Phosphotyrosine; by FYN => ECO:0000269|PubMed:19652227
ChainResidueDetails
ATYR32
BTYR32

site_idSWS_FT_FI2
Number of Residues2
DetailsMOD_RES: N6-succinyllysine => ECO:0000250|UniProtKB:O08553
ChainResidueDetails
ALYS258
BLYS258

site_idSWS_FT_FI3
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P47942
ChainResidueDetails
ASER259
BSER259

site_idSWS_FT_FI4
Number of Residues2
DetailsMOD_RES: Phosphotyrosine => ECO:0000250|UniProtKB:O08553
ChainResidueDetails
ATYR431
BTYR431

site_idSWS_FT_FI5
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:O08553
ChainResidueDetails
ASER465
BSER465

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PDB entries from 2024-09-11

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